1yxd

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[[Image:1yxd.png|left|200px]]
 
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{{STRUCTURE_1yxd| PDB=1yxd | SCENE= }}
{{STRUCTURE_1yxd| PDB=1yxd | SCENE= }}
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===Structure of E. coli dihydrodipicolinate synthase bound with allosteric inhibitor (S)-lysine to 2.0 A===
===Structure of E. coli dihydrodipicolinate synthase bound with allosteric inhibitor (S)-lysine to 2.0 A===
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{{ABSTRACT_PUBMED_16041077}}
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{{ABSTRACT_PUBMED_16041077}}
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==Function==
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[[http://www.uniprot.org/uniprot/DAPA_ECOLI DAPA_ECOLI]] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).<ref>PMID:20503968</ref> <ref>PMID:8993314</ref>
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:016041077</ref><references group="xtra"/>
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<ref group="xtra">PMID:016041077</ref><references group="xtra"/><references/>
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[[Category: Dihydrodipicolinate synthase]]
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[[Category: 4-hydroxy-tetrahydrodipicolinate synthase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Dobson, R C.J.]]
[[Category: Dobson, R C.J.]]

Revision as of 05:20, 28 August 2013

Template:STRUCTURE 1yxd

Contents

Structure of E. coli dihydrodipicolinate synthase bound with allosteric inhibitor (S)-lysine to 2.0 A

Template:ABSTRACT PUBMED 16041077

Function

[DAPA_ECOLI] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).[1] [2]

About this Structure

1yxd is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.

See Also

Reference

  • Dobson RC, Griffin MD, Jameson GB, Gerrard JA. The crystal structures of native and (S)-lysine-bound dihydrodipicolinate synthase from Escherichia coli with improved resolution show new features of biological significance. Acta Crystallogr D Biol Crystallogr. 2005 Aug;61(Pt 8):1116-24. Epub 2005, Jul 20. PMID:16041077 doi:10.1107/S0907444905016318
  1. ↑ Devenish SR, Blunt JW, Gerrard JA. NMR studies uncover alternate substrates for dihydrodipicolinate synthase and suggest that dihydrodipicolinate reductase is also a dehydratase. J Med Chem. 2010 Jun 24;53(12):4808-12. doi: 10.1021/jm100349s. PMID:20503968 doi:10.1021/jm100349s
  2. ↑ Blickling S, Renner C, Laber B, Pohlenz HD, Holak TA, Huber R. Reaction mechanism of Escherichia coli dihydrodipicolinate synthase investigated by X-ray crystallography and NMR spectroscopy. Biochemistry. 1997 Jan 7;36(1):24-33. PMID:8993314 doi:10.1021/bi962272d

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