3gmt

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[[Image:3gmt.png|left|200px]]
 
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{{STRUCTURE_3gmt| PDB=3gmt | SCENE= }}
{{STRUCTURE_3gmt| PDB=3gmt | SCENE= }}
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===Crystal structure of adenylate kinase from burkholderia pseudomallei===
===Crystal structure of adenylate kinase from burkholderia pseudomallei===
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{{ABSTRACT_PUBMED_20331978}}
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{{ABSTRACT_PUBMED_20331978}}
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==Function==
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[[http://www.uniprot.org/uniprot/KAD_BURP1 KAD_BURP1]] Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism (By similarity).
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:020331978</ref><references group="xtra"/>
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<ref group="xtra">PMID:020331978</ref><references group="xtra"/><references/>
[[Category: Adenylate kinase]]
[[Category: Adenylate kinase]]
[[Category: Burkholderia pseudomallei 1710b]]
[[Category: Burkholderia pseudomallei 1710b]]

Revision as of 08:33, 30 October 2013

Template:STRUCTURE 3gmt

Contents

Crystal structure of adenylate kinase from burkholderia pseudomallei

Template:ABSTRACT PUBMED 20331978

Function

[KAD_BURP1] Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism (By similarity).

About this Structure

3gmt is a 2 chain structure with sequence from Burkholderia pseudomallei 1710b. Full crystallographic information is available from OCA.

See Also

Reference

  • Buchko GW, Robinson H, Abendroth J, Staker BL, Myler PJ. Structural characterization of Burkholderia pseudomallei adenylate kinase (Adk): profound asymmetry in the crystal structure of the 'open' state. Biochem Biophys Res Commun. 2010 Apr 16;394(4):1012-7. Epub 2010 Mar 21. PMID:20331978 doi:10.1016/j.bbrc.2010.03.112

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