NDLI: Crystal Structure of Cryptosporidium parvum Pyruvate Kinase

Content Provider	PubMed Central
Author	Cook, William J. Olga, Senkovich Aleem, Khadijah Chattopadhyay, Debasish
Editor	Kursula, Inari
Copyright Year	2012
Abstract	Pyruvate kinase plays a critical role in cellular metabolism of glucose by serving as a major regulator of glycolysis. This tetrameric enzyme is allosterically regulated by different effector molecules, mainly phosphosugars. In response to binding of effector molecules and substrates, significant structural changes have been identified in various pyruvate kinase structures. Pyruvate kinase of Cryptosporidium parvum is exceptional among known enzymes of protozoan origin in that it exhibits no allosteric property in the presence of commonly known effector molecules. The crystal structure of pyruvate kinase from C. parvum has been solved by molecular replacement techniques and refined to 2.5 Å resolution. In the active site a glycerol molecule is located near the γ-phosphate site of ATP, and the protein structure displays a partially closed active site. However, unlike other structures where the active site is closed, the α6' helix in C. parvum pyruvate kinase unwinds and assumes an extended conformation. In the crystal structure a sulfate ion is found at a site that is occupied by a phosphate of the effector molecule in many pyruvate kinase structures. A new feature of the C. parvum pyruvate kinase structure is the presence of a disulfide bond cross-linking the two monomers in the asymmetric unit. The disulfide bond is formed between cysteine residue 26 in the short N-helix of one monomer with cysteine residue 312 in a long helix (residues 303–320) of the second monomer at the interface of these monomers. Both cysteine residues are unique to C. parvum, and the disulfide bond remained intact in a reduced environment. However, the significance of this bond, if any, remains unknown at this time.
Related Links	http://dx.doi.org/10.1371/journal.pone.0046875
Starting Page	46875
File Format	PDF
ISSN	19326203
e-ISSN	19326203
Journal	PLoS ONE
Issue Number	10
Volume Number	7
Language	English
Publisher	Public Library of Science
Publisher Date	2012-10-01
Access Restriction	Open
Rights Holder	Public Library of Science
Subject Keyword	Biochemistry, Genetics and Molecular Biology(all) Agricultural and Biological Sciences(all) Medicine(all) 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

The Crystal Structure of Toxoplasma gondii Pyruvate Kinase 1

The Cryptosporidium Parvum Transcriptome during In Vitro Development

Characterization of 14-3-3 Proteins from Cryptosporidium parvum

Intra-Species Diversity and Panmictic Structure of Cryptosporidium parvum Populations in Cattle Farms in Northern Spain

Detection of Cryptosporidium parvum Oocysts on Fresh Produce Using DNA Aptamers

SHP-2 Mediates Cryptosporidium parvum Infectivity in Human Intestinal Epithelial Cells

Crystal Structure of the N-Acetylmannosamine Kinase Domain of GNE

Multilocus Sequence Subtyping and Genetic Structure of Cryptosporidium muris and Cryptosporidium andersoni

Isoform Switch of Pyruvate Kinase M1 Indeed Occurs but Not to Pyruvate Kinase M2 in Human Tumorigenesis

Crystal Structure of Cryptosporidium parvum Pyruvate Kinase

Similar Documents

The Crystal Structure of Toxoplasma gondii Pyruvate Kinase 1

The Cryptosporidium Parvum Transcriptome during In Vitro Development

Characterization of 14-3-3 Proteins from Cryptosporidium parvum

Intra-Species Diversity and Panmictic Structure of Cryptosporidium parvum Populations in Cattle Farms in Northern Spain

Detection of Cryptosporidium parvum Oocysts on Fresh Produce Using DNA Aptamers

SHP-2 Mediates Cryptosporidium parvum Infectivity in Human Intestinal Epithelial Cells

Crystal Structure of the N-Acetylmannosamine Kinase Domain of GNE

Multilocus Sequence Subtyping and Genetic Structure of Cryptosporidium muris and Cryptosporidium andersoni

Isoform Switch of Pyruvate Kinase M1 Indeed Occurs but Not to Pyruvate Kinase M2 in Human Tumorigenesis

Crystal Structure of Cryptosporidium parvum Pyruvate Kinase