NDLI: Structural and biochemical implications of single amino acid substitutions in the nucleotide-dependent switch regions of the nitrogenase Fe protein from Azotobacter vinelandii

Please wait, while we are loading the content...

Quantification of isomeric equilibria formed by metal ion complexes of 8-[2-(phosphonomethoxy)ethyl]-8-azaadenine (8,8aPMEA) and 9-[2-(phosphonomethoxy)ethyl]-8-azaadenine (9,8aPMEA). Derivatives of the antiviral nucleotide analogue 9-[2-(phosphonomethoxy)ethyl]adenine (PMEA)

IR and Raman study on the interactions of the 5′-GMP and 5′-CMP phosphate groups with Mg(II), Ca(II), Sr(II), Ba(II), Cr(III), Co(II), Cu(II), Zn(II), Cd(II), Al(III) and Ga(III)

Studies on the degradation pathway of iron-sulfur centers during unfolding of a hyperstable ferredoxin: cluster dissociation, iron release and protein stability

The 40s Ω-loop plays a critical role in the stability and the alkaline conformational transition of cytochrome c

Direct monitoring of the electron pool effect of cytochrome c3 by highly sensitive EQCM measurements

Miniaturized heme proteins: crystal structure of Co(III)-mimochrome IV

Structural and biochemical implications of single amino acid substitutions in the nucleotide-dependent switch regions of the nitrogenase Fe protein from Azotobacter vinelandii

Structure and binding of Mg(II) ions and di-metal bridge complexes with biological phosphates and phosphoranes

JBIC Journal of Biological Inorganic Chemistry : Volume 9, Issue 7, October 2004

JBIC Journal of Biological Inorganic Chemistry : Volume 9, Issue 6, September 2004

JBIC Journal of Biological Inorganic Chemistry : Volume 9, Issue 5, July 2004

JBIC Journal of Biological Inorganic Chemistry : Volume 9, Issue 4, June 2004

JBIC Journal of Biological Inorganic Chemistry : Volume 9, Issue 3, April 2004

JBIC Journal of Biological Inorganic Chemistry : Volume 9, Issue 2, March 2004

JBIC Journal of Biological Inorganic Chemistry : Volume 9, Issue 1, January 2004

JBIC Journal of Biological Inorganic Chemistry : Volume 8

JBIC Journal of Biological Inorganic Chemistry : Volume 7

JBIC Journal of Biological Inorganic Chemistry : Volume 6

JBIC Journal of Biological Inorganic Chemistry : Volume 5

JBIC Journal of Biological Inorganic Chemistry : Volume 4

JBIC Journal of Biological Inorganic Chemistry : Volume 3

JBIC Journal of Biological Inorganic Chemistry : Volume 2

Structural and biochemical implications of single amino acid substitutions in the nucleotide-dependent switch regions of the nitrogenase Fe protein from Azotobacter vinelandii

Content Provider	Springer Nature Link
Author	Jang, Se Bok Jeong, Mi Suk Seefeldt, Lance C. Peters, John W.
Copyright Year	2004
Abstract	The structures of nitrogenase Fe proteins with defined amino acid substitutions in the previously implicated nucleotide-dependent signal transduction pathways termed switch I and switch II have been determined by X-ray diffraction methods. In the Fe protein of nitrogenase the nucleotide-dependent switch regions are responsible for communication between the sites responsible for nucleotide binding and hydrolysis and the [4Fe-4S] cluster of the Fe protein and the docking interface that interacts with the MoFe protein upon macromolecular complex formation. In this study the structural characterization of the Azotobacter vinelandii nitrogenase Fe protein with Asp at position 39 substituted by Asn in MgADP-bound and nucleotide-free states provides an explanation for the experimental observation that the altered Fe proteins form a trapped complex subsequent to a single electron transfer event. The structures reveal that the substitution allows the formation of a hydrogen bond between the switch I Asn39 and the switch II Asp125. In the structure of the native enzyme the analogous interaction between the side chains of Asp39 and Asp125 is precluded due to electrostatic repulsion. These results suggest that the electrostatic repulsion between Asp39 and Asp125 is important for dissociation of the Fe protein:MoFe protein complex during catalysis. In a separate study, the structural characterization of the Fe protein with Asp129 substituted by Glu provides the structural basis for the observation that the Glu129-substituted variant in the absence of bound nucleotides has biochemical properties in common with the native Fe protein with bound MgADP. Interactions of the longer Glu side chain with the phosphate binding loop (P-loop) results in a similar conformation of the switch II region as the conformation that results from the binding of the phosphate of ADP to the P-loop.
Starting Page	1028
Ending Page	1033
Page Count	6
File Format	PDF
ISSN	09498257
Journal	JBIC Journal of Biological Inorganic Chemistry
Volume Number	9
Issue Number	8
e-ISSN	14321327
Language	English
Publisher	Springer-Verlag
Publisher Date	2004-11-10
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	[FeS] cluster Iron protein Signal transduction
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

The amino acid sequence of the nitrogenase iron protein from Azotobacter vinelandii.

Selenocyanate derived Se-incorporation into the nitrogenase Fe protein cluster

Selenocyanate derived Se-incorporation into the nitrogenase Fe protein cluster.

Kinetics of MgATP-dependent iron chelation from the Fe-protein of the Azotobacter vinelandii nitrogenase complex. Evidence for two states.

Iron EXAFS of Azotobacter vinelandii Nitrogenase Mo-Fe (1992)

EPR and Mössbauer studies of nucleotide-bound nitrogenase iron protein from Azotobacter vinelandii.

Evidence That MgATP Accelerates Primary Electron Transfer in aClostridium pasteurianum Fe Protein-Azotobacter vinelandii MoFe Protein Nitrogenase Tight Complex

Electron microscopy of the Mo-Fe-protein from Azotobacter vinelandii nitrogenase

Crystallization of the Azotobacter vinelandii nitrogenase iron protein.

Structural and biochemical implications of single amino acid substitutions in the nucleotide-dependent switch regions of the nitrogenase Fe protein from Azotobacter vinelandii

Similar Documents

The amino acid sequence of the nitrogenase iron protein from Azotobacter vinelandii.

Selenocyanate derived Se-incorporation into the nitrogenase Fe protein cluster

Selenocyanate derived Se-incorporation into the nitrogenase Fe protein cluster.

Kinetics of MgATP-dependent iron chelation from the Fe-protein of the Azotobacter vinelandii nitrogenase complex. Evidence for two states.

Iron EXAFS of Azotobacter vinelandii Nitrogenase Mo-Fe (1992)

EPR and Mössbauer studies of nucleotide-bound nitrogenase iron protein from Azotobacter vinelandii.

Evidence That MgATP Accelerates Primary Electron Transfer in aClostridium pasteurianum Fe Protein-Azotobacter vinelandii MoFe Protein Nitrogenase Tight Complex

Electron microscopy of the Mo-Fe-protein from Azotobacter vinelandii nitrogenase

Crystallization of the Azotobacter vinelandii nitrogenase iron protein.

Structural and biochemical implications of single amino acid substitutions in the nucleotide-dependent switch regions of the nitrogenase Fe protein from Azotobacter vinelandii