1vm6

Crystal structure of Dihydrodipicolinate reductase (TM1520) from Thermotoga maritima at 2.27 A resolutionCrystal structure of Dihydrodipicolinate reductase (TM1520) from Thermotoga maritima at 2.27 A resolution

Structural highlights

1vm6 is a 4 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.27Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

DAPB_THEMA Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate (Probable). Uses NADPH as a reductant with much more efficiency than NADH.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

↑ Pearce FG, Sprissler C, Gerrard JA. Characterization of dihydrodipicolinate reductase from Thermotoga maritima reveals evolution of substrate binding kinetics. J Biochem. 2008 May;143(5):617-23. doi: 10.1093/jb/mvn012. Epub 2008 Feb 4. PMID:18250105 doi:http://dx.doi.org/10.1093/jb/mvn012

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OCA

[1] Pearce FG, Sprissler C, Gerrard JA. Characterization of dihydrodipicolinate reductase from Thermotoga maritima reveals evolution of substrate binding kinetics. J Biochem. 2008 May;143(5):617-23. doi: 10.1093/jb/mvn012. Epub 2008 Feb 4. PMID:18250105 doi:http://dx.doi.org/10.1093/jb/mvn012

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