2ews

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|PDB= 2ews |SIZE=350|CAPTION= <scene name='initialview01'>2ews</scene>, resolution 2.05&Aring;
|PDB= 2ews |SIZE=350|CAPTION= <scene name='initialview01'>2ews</scene>, resolution 2.05&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER'>ANP</scene>
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|LIGAND= <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Pantothenate_kinase Pantothenate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.33 2.7.1.33]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Pantothenate_kinase Pantothenate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.33 2.7.1.33] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ews FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ews OCA], [http://www.ebi.ac.uk/pdbsum/2ews PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ews RCSB]</span>
}}
}}
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[[Category: Park, H W.]]
[[Category: Park, H W.]]
[[Category: SGC, Structural Genomics Consortium.]]
[[Category: SGC, Structural Genomics Consortium.]]
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[[Category: ANP]]
 
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[[Category: MG]]
 
[[Category: pank]]
[[Category: pank]]
[[Category: sgc]]
[[Category: sgc]]
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[[Category: structural genomics consortium]]
[[Category: structural genomics consortium]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:45:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:54:54 2008''

Revision as of 23:54, 30 March 2008


PDB ID 2ews

Drag the structure with the mouse to rotate
, resolution 2.05Å
Ligands: ,
Activity: Pantothenate kinase, with EC number 2.7.1.33
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of S.aureus pantothenate kinase


Overview

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.

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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