2ews

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(New page: 200px<br /><applet load="2ews" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ews, resolution 2.05&Aring;" /> '''Crystal structure of...)
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[[Image:2ews.jpg|left|200px]]<br /><applet load="2ews" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2ews, resolution 2.05&Aring;" />
caption="2ews, resolution 2.05&Aring;" />
'''Crystal structure of S.aureus pantothenate kinase'''<br />
'''Crystal structure of S.aureus pantothenate kinase'''<br />
==Overview==
==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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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==
==About this Structure==
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2EWS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with MG and ANP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2EWS OCA].
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2EWS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ANP:'>ANP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EWS OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
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[[Category: Hong, B.S.]]
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[[Category: Hong, B S.]]
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[[Category: Park, H.W.]]
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[[Category: Park, H W.]]
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[[Category: SGC, Structural.Genomics.Consortium.]]
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[[Category: SGC, Structural Genomics Consortium.]]
[[Category: ANP]]
[[Category: ANP]]
[[Category: MG]]
[[Category: MG]]
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[[Category: structural genomics consortium]]
[[Category: structural genomics consortium]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:11:45 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:15:21 2008''

Revision as of 15:15, 21 February 2008


2ews, resolution 2.05Å

Drag the structure with the mouse to rotate

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 with and as ligands. Active as Pantothenate kinase, with EC number 2.7.1.33 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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