2h2w

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Crystal structure of Homoserine O-succinyltransferase (EC 2.3.1.46) (Homoserine O-transsuccinylase) (HTS) (tm0881) from THERMOTOGA MARITIMA at 2.52 A resolutionCrystal structure of Homoserine O-succinyltransferase (EC 2.3.1.46) (Homoserine O-transsuccinylase) (HTS) (tm0881) from THERMOTOGA MARITIMA at 2.52 A resolution

Structural highlights

2h2w is a 1 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 2.52Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

METAA_THEMA Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine. Utilizes a ping-pong kinetic mechanism in which the acetyl group of acetyl-CoA is initially transferred to the enzyme to form an acetyl-enzyme intermediate before subsequent transfer to homoserine to form the final product, O-acetylhomoserine. Has weak activity with succinyl-CoA as the acyl donor.[1]

Evolutionary Conservation

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

References

  1. Goudarzi M, Born TL. Purification and characterization of Thermotoga maritima homoserine transsuccinylase indicates it is a transacetylase. Extremophiles. 2006 Oct;10(5):469-78. doi: 10.1007/s00792-006-0522-3. Epub 2006 , May 18. PMID:16708165 doi:http://dx.doi.org/10.1007/s00792-006-0522-3

2h2w, resolution 2.52Å

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OCA