3wdm

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'''Unreleased structure'''
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{{STRUCTURE_3wdm| PDB=3wdm | SCENE= }}
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===Crystal structure of 4-phosphopantoate-beta-alanine ligase from Thermococcus kodakarensis===
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{{ABSTRACT_PUBMED_24638914}}
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The entry 3wdm is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/PPS_THEKO PPS_THEKO]] Catalyzes the conversion of (R)-4-phosphopantoate and beta-alanine to 4'-phosphopantothenate in the CoA biosynthesis pathway. Cannot use (R)-pantoate as substrate and thus does not display pantothenate synthetase (PS) activity.
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Authors: Kishimoto, A., Kita, A., Ishibashi, T., Tomita, H., Yokooji, Y., Imanaka, T., Atomi, H., Miki, K.
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==About this Structure==
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[[3wdm]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WDM OCA].
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Description: Crystal structure of 4-phosphopantoate-beta-alanine ligase from Thermococcus kodakarensis
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==Reference==
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<ref group="xtra">PMID:024638914</ref><references group="xtra"/><references/>
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[[Category: 4-phosphopantoate--beta-alanine ligase]]
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[[Category: Atomi, H.]]
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[[Category: Imanaka, T.]]
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[[Category: Ishibashi, T.]]
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[[Category: Kishimoto, A.]]
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[[Category: Kita, A.]]
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[[Category: Miki, K.]]
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[[Category: Tomita, H.]]
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[[Category: Yokooji, Y.]]
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[[Category: Ligase]]

Revision as of 09:17, 2 April 2014

Template:STRUCTURE 3wdm

Contents

Crystal structure of 4-phosphopantoate-beta-alanine ligase from Thermococcus kodakarensis

Template:ABSTRACT PUBMED 24638914

Function

[PPS_THEKO] Catalyzes the conversion of (R)-4-phosphopantoate and beta-alanine to 4'-phosphopantothenate in the CoA biosynthesis pathway. Cannot use (R)-pantoate as substrate and thus does not display pantothenate synthetase (PS) activity.

About this Structure

3wdm is a 4 chain structure. Full crystallographic information is available from OCA.

Reference

  • Kishimoto A, Kita A, Ishibashi T, Tomita H, Yokooji Y, Imanaka T, Atomi H, Miki K. Crystal Structure of Phosphopantothenate Synthetase from Thermococcus k odakarensis. Proteins. 2014 Mar 17. doi: 10.1002/prot.24546. PMID:24638914 doi:http://dx.doi.org/10.1002/prot.24546

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