3kem

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{{STRUCTURE_3kem| PDB=3kem | SCENE= }}
{{STRUCTURE_3kem| PDB=3kem | SCENE= }}
===Crystal structure of IspH:IPP complex===
===Crystal structure of IspH:IPP complex===
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{{ABSTRACT_PUBMED_020080550}}
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{{ABSTRACT_PUBMED_20080550}}
==Function==
==Function==
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==About this Structure==
==About this Structure==
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[[3kem]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KEM OCA].
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[[3kem]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KEM OCA].
==Reference==
==Reference==
<ref group="xtra">PMID:020080550</ref><references group="xtra"/><references/>
<ref group="xtra">PMID:020080550</ref><references group="xtra"/><references/>
[[Category: 4-hydroxy-3-methylbut-2-enyl diphosphate reductase]]
[[Category: 4-hydroxy-3-methylbut-2-enyl diphosphate reductase]]
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[[Category: Escherichia coli]]
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[[Category: Ecoli]]
[[Category: Bacher, A.]]
[[Category: Bacher, A.]]
[[Category: Eisenreich, W.]]
[[Category: Eisenreich, W.]]

Revision as of 05:54, 4 December 2013

Template:STRUCTURE 3kem

Contents

Crystal structure of IspH:IPP complex

Template:ABSTRACT PUBMED 20080550

Function

[ISPH_ECOLI] Converts 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Is also involved in penicillin tolerance and control of the stringent response. Seems to directly or indirectly interact with RelA to maintain it in an inactive form during normal growth.[1] [2] [3]

About this Structure

3kem is a 2 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA.

Reference

  • Grawert T, Span I, Eisenreich W, Rohdich F, Eppinger J, Bacher A, Groll M. Probing the reaction mechanism of IspH protein by x-ray structure analysis. Proc Natl Acad Sci U S A. 2010 Jan 19;107(3):1077-81. Epub 2009 Dec 28. PMID:20080550
  1. ↑ Grawert T, Rohdich F, Span I, Bacher A, Eisenreich W, Eppinger J, Groll M. Structure of active IspH enzyme from Escherichia coli provides mechanistic insights into substrate reduction. Angew Chem Int Ed Engl. 2009;48(31):5756-9. PMID:19569147 doi:10.1002/anie.200900548
  2. ↑ Grawert T, Span I, Eisenreich W, Rohdich F, Eppinger J, Bacher A, Groll M. Probing the reaction mechanism of IspH protein by x-ray structure analysis. Proc Natl Acad Sci U S A. 2010 Jan 19;107(3):1077-81. Epub 2009 Dec 28. PMID:20080550
  3. ↑ Span I, Grawert T, Bacher A, Eisenreich W, Groll M. Crystal Structures of Mutant IspH Proteins Reveal a Rotation of the Substrate's Hydroxymethyl Group during Catalysis. J Mol Biol. 2011 Nov 23. PMID:22137895 doi:10.1016/j.jmb.2011.11.033

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