NDLI: Crystal Structure of Human Protein N-Terminal Glutamine Amidohydrolase, an Initial Component of the N-End Rule Pathway

Content Provider	PubMed Central
Author	Park, Mi Seul Bitto, Eduard Kim, Kyung Rok Bingman, Craig A. Miller, Mitchell D. Kim, Hyun-jung Han, Byung Woo Phillips, George N.
Editor	Boggon, Titus J.
Copyright Year	2014
Abstract	The N-end rule states that half-life of protein is determined by their N-terminal amino acid residue. N-terminal glutamine amidohydrolase (Ntaq) converts N-terminal glutamine to glutamate by eliminating the amine group and plays an essential role in the N-end rule pathway for protein degradation. Here, we report the crystal structure of human Ntaq1 bound with the N-terminus of a symmetry-related Ntaq1 molecule at 1.5 Å resolution. The structure reveals a monomeric globular protein with alpha-beta-alpha three-layer sandwich architecture. The catalytic triad located in the active site, Cys-His-Asp, is highly conserved among Ntaq family and transglutaminases from diverse organisms. The N-terminus of a symmetry-related Ntaq1 molecule bound in the substrate binding cleft and the active site suggest possible substrate binding mode of hNtaq1. Based on our crystal structure of hNtaq1 and docking study with all the tripeptides with N-terminal glutamine, we propose how the peptide backbone recognition patch of hNtaq1 forms nonspecific interactions with N-terminal peptides of substrate proteins. Upon binding of a substrate with N-terminal glutamine, active site catalytic triad mediates the deamination of the N-terminal residue to glutamate by a mechanism analogous to that of cysteine proteases.
Related Links	http://dx.doi.org/10.1371/journal.pone.0111142
Starting Page	111142
File Format	PDF
ISSN	19326203
e-ISSN	19326203
Journal	PLoS ONE
Issue Number	10
Volume Number	9
Language	English
Publisher	Public Library of Science
Publisher Date	2014-10-30
Access Restriction	Open
Rights Holder	Public Library of Science
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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

Glutamine-Specific N-Terminal Amidase, a Component of the N-End Rule Pathway

The Sequence of Porcine Protein NH-terminal Asparagine Amidohydrolase A NEW COMPONENT OF THE N-END RULE PATHWAY

The mouse and human genes encoding the recognition component of the N-end rule pathway

PRT1 of Arabidopsis thaliana encodes a component of the plant N-end rule pathway

Control of mammalian G protein signaling by N-terminal acetylationand the N-end rule pathway

N-terminal acetylation and the N-end rule pathway control degradation of the lipid droplet protein PLIN2

N-terminal methionine excision of proteins creates tertiary destabilizing N-degrons of the Arg/N-end rule pathway

N-Terminal Acetylation-Targeted N-End Rule Proteolytic System: The Ac/N-End Rule Pathway

Yeast N-terminal Amidase A NEW ENZYME AND COMPONENT OF THE N-END RULE PATHWAY

Crystal Structure of Human Protein N-Terminal Glutamine Amidohydrolase, an Initial Component of the N-End Rule Pathway

Similar Documents

Glutamine-Specific N-Terminal Amidase, a Component of the N-End Rule Pathway

The Sequence of Porcine Protein NH-terminal Asparagine Amidohydrolase A NEW COMPONENT OF THE N-END RULE PATHWAY

The mouse and human genes encoding the recognition component of the N-end rule pathway

PRT1 of Arabidopsis thaliana encodes a component of the plant N-end rule pathway

Control of mammalian G protein signaling by N-terminal acetylationand the N-end rule pathway

N-terminal acetylation and the N-end rule pathway control degradation of the lipid droplet protein PLIN2

N-terminal methionine excision of proteins creates tertiary destabilizing N-degrons of the Arg/N-end rule pathway

N-Terminal Acetylation-Targeted N-End Rule Proteolytic System: The Ac/N-End Rule Pathway

Yeast N-terminal Amidase A NEW ENZYME AND COMPONENT OF THE N-END RULE PATHWAY

Crystal Structure of Human Protein N-Terminal Glutamine Amidohydrolase, an Initial Component of the N-End Rule Pathway