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3rmj
From Proteopedia
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{{STRUCTURE_3rmj| PDB=3rmj | SCENE= }} | {{STRUCTURE_3rmj| PDB=3rmj | SCENE= }} | ||
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===Crystal structure of truncated alpha-Isopropylmalate Synthase from Neisseria meningitidis=== | ===Crystal structure of truncated alpha-Isopropylmalate Synthase from Neisseria meningitidis=== | ||
| + | {{ABSTRACT_PUBMED_22352945}} | ||
| - | + | ==Function== | |
| - | + | [[http://www.uniprot.org/uniprot/LEU1_NEIMB LEU1_NEIMB]] Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate) (By similarity). | |
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==About this Structure== | ==About this Structure== | ||
| - | [[3rmj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | [[3rmj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Neimi Neimi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RMJ OCA]. |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:022352945</ref><references group="xtra"/> | + | <ref group="xtra">PMID:022352945</ref><references group="xtra"/><references/> |
[[Category: 2-isopropylmalate synthase]] | [[Category: 2-isopropylmalate synthase]] | ||
| - | [[Category: | + | [[Category: Neimi]] |
[[Category: Baker, E N.]] | [[Category: Baker, E N.]] | ||
[[Category: Baker, H M.]] | [[Category: Baker, H M.]] | ||
Revision as of 14:16, 12 March 2014
Contents |
Crystal structure of truncated alpha-Isopropylmalate Synthase from Neisseria meningitidis
Template:ABSTRACT PUBMED 22352945
Function
[LEU1_NEIMB] Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate) (By similarity).
About this Structure
3rmj is a 2 chain structure with sequence from Neimi. Full crystallographic information is available from OCA.
Reference
- Huisman FH, Koon N, Bulloch EM, Baker HM, Baker EN, Squire CJ, Parker EJ. Removal of the C-Terminal Regulatory Domain of alpha-Isopropylmalate Synthase Disrupts Functional Substrate Binding. Biochemistry. 2012 Mar 6. PMID:22352945 doi:10.1021/bi201717j
