4oca

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m (Protected "4oca" [edit=sysop:move=sysop])
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'''Unreleased structure'''
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{{STRUCTURE_4oca| PDB=4oca | SCENE= }}
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===Cryatal structure of ArnB K188A complexted with PLP and UDP-Ara4N===
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{{ABSTRACT_PUBMED_24460375}}
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The entry 4oca is ON HOLD
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==Function==
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[[http://www.uniprot.org/uniprot/F5ZUF5_SALTU F5ZUF5_SALTU]] Catalyzes the conversion of UDP-4-keto-arabinose (UDP-Ara4O) to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides (By similarity).[HAMAP-Rule:MF_01167][SAAS:SAAS022850_004_033570]
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Authors: Sousa, M.C., Lee, M.
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==About this Structure==
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[[4oca]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OCA OCA].
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Description: Cryatal structure of ArnB K188A complexted with PLP and UDP-Ara4N
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==Reference==
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<ref group="xtra">PMID:024460375</ref><references group="xtra"/><references/>
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[[Category: UDP-4-amino-4-deoxy-L-arabinose aminotransferase]]
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[[Category: Lee, M.]]
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[[Category: Sousa, M C.]]
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[[Category: Aminotransferase]]
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[[Category: Transferase]]

Revision as of 13:30, 12 March 2014

Template:STRUCTURE 4oca

Contents

Cryatal structure of ArnB K188A complexted with PLP and UDP-Ara4N

Template:ABSTRACT PUBMED 24460375

Function

[F5ZUF5_SALTU] Catalyzes the conversion of UDP-4-keto-arabinose (UDP-Ara4O) to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides (By similarity).[HAMAP-Rule:MF_01167][SAAS:SAAS022850_004_033570]

About this Structure

4oca is a 1 chain structure. Full crystallographic information is available from OCA.

Reference

  • Lee M, Sousa MC. Structural Basis for Substrate Specificity in ArnB. A Key Enzyme in the Polymyxin Resistance Pathway of Gram-Negative Bacteria. Biochemistry. 2014 Feb 4;53(4):796-805. doi: 10.1021/bi4015677. Epub 2014 Jan 24. PMID:24460375 doi:http://dx.doi.org/10.1021/bi4015677

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OCA

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