2ews

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[[Image:2ews.jpg|left|200px]]
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{{Seed}}
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{{STRUCTURE_2ews| PDB=2ews | SCENE= }}
{{STRUCTURE_2ews| PDB=2ews | SCENE= }}
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'''Crystal structure of S.aureus pantothenate kinase'''
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===Crystal structure of S.aureus pantothenate kinase===
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==Overview==
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Three distinct isoforms of pantothenate kinase (CoaA) in bacteria catalyze the first step in coenzyme A biosynthesis. The structures of the type II (Staphylococcus aureus, SaCoaA) and type III (Pseudomonas aeruginosa, PaCoaA) enzymes reveal that they assemble nearly identical subunits with actin-like folds into dimers that exhibit distinct biochemical properties. PaCoaA has a fully enclosed pantothenate binding pocket and requires a monovalent cation to weakly bind ATP in an open cavity that does not interact with the adenine nucleotide. Pantothenate binds to an open pocket in SaCoaA that strongly binds ATP by using a classical P loop architecture coupled with specific interactions with the adenine moiety. The PaCoaA*Pan binary complex explains the resistance of bacteria possessing this isoform to the pantothenamide antibiotics, and the similarity between SaCoaA and human pantothenate kinase 2 explains the molecular basis for the development of the neurodegenerative phenotype in three mutations in the human protein.
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(as it appears on PubMed at http://www.pubmed.gov), where 16905099 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16905099}}
==About this Structure==
==About this Structure==
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[[Category: Structural genomic]]
[[Category: Structural genomic]]
[[Category: Structural genomics consortium]]
[[Category: Structural genomics consortium]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:12:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:04:45 2008''

Revision as of 05:04, 29 July 2008

Template:STRUCTURE 2ews

Crystal structure of S.aureus pantothenate kinase

Template:ABSTRACT PUBMED 16905099

About this Structure

2EWS is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

Reference

Prokaryotic type II and type III pantothenate kinases: The same monomer fold creates dimers with distinct catalytic properties., Hong BS, Yun MK, Zhang YM, Chohnan S, Rock CO, White SW, Jackowski S, Park HW, Leonardi R, Structure. 2006 Aug;14(8):1251-61. PMID:16905099

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