3vfl

Structure, Function, Stability and Knockout Phenotype of Dihydrodipicolinate Synthase from Streptococcus pneumoniaeStructure, Function, Stability and Knockout Phenotype of Dihydrodipicolinate Synthase from Streptococcus pneumoniae

Template:ABSTRACT PUBMED 20057065

FunctionFunction

[A5LD17_STREE] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA) (By similarity).[HAMAP-Rule:MF_00418][SAAS:SAAS005263_004_011311]

About this StructureAbout this Structure

3vfl is a 2 chain structure with sequence from Streptococcus pneumoniae sp3-bs71. This structure supersedes the now removed PDB entry 3h5d. Full crystallographic information is available from OCA.

ReferenceReference

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↑ Sibarani NE, Gorman MA, Dogovski C, Parker MW, Perugini MA. Crystallization of dihydrodipicolinate synthase from a clinical isolate of Streptococcus pneumoniae. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jan 1;66(Pt, 1):32-6. Epub 2009 Dec 25. PMID:20057065 doi:10.1107/S174430910904771X

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OCA

[1] Sibarani NE, Gorman MA, Dogovski C, Parker MW, Perugini MA. Crystallization of dihydrodipicolinate synthase from a clinical isolate of Streptococcus pneumoniae. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jan 1;66(Pt, 1):32-6. Epub 2009 Dec 25. PMID:20057065 doi:10.1107/S174430910904771X

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