2ctz

Crystal structure of o-acetyl homoserine sulfhydrylase from Thermus thermophilus HB8Crystal structure of o-acetyl homoserine sulfhydrylase from Thermus thermophilus HB8

Structural highlights

2ctz is a 2 chain structure with sequence from Thermus thermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.6Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

METY1_THET8 Catalyzes the conversion of O-acetyl-L-homoserine (OAH) into homocysteine in the methionine biosynthesis pathway. Has weak activity with O-acetyl-L-serine, O-phospho-L-serine, L-serine, O-succinyl-L-homoserine and L-homoserine. Shows low CTT beta-lyase activity and very low CTT gamma-synthase activity.^[1]

Evolutionary Conservation

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

References

↑ Shimizu H, Yamagata S, Masui R, Inoue Y, Shibata T, Yokoyama S, Kuramitsu S, Iwama T. Cloning and overexpression of the oah1 gene encoding O-acetyl-L-homoserine sulfhydrylase of Thermus thermophilus HB8 and characterization of the gene product. Biochim Biophys Acta. 2001 Sep 10;1549(1):61-72. PMID:11566369 doi:10.1016/s0167-4838(01)00245-x

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OCA

[1] Shimizu H, Yamagata S, Masui R, Inoue Y, Shibata T, Yokoyama S, Kuramitsu S, Iwama T. Cloning and overexpression of the oah1 gene encoding O-acetyl-L-homoserine sulfhydrylase of Thermus thermophilus HB8 and characterization of the gene product. Biochim Biophys Acta. 2001 Sep 10;1549(1):61-72. PMID:11566369 doi:10.1016/s0167-4838(01)00245-x

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