2ztj

From Proteopedia

Jump to: navigation, search

Crystal structure of homocitrate synthase from Thermus thermophilus complexed with alpha-ketoglutarate

Structural highlights

2ztj is a 1 chain structure with sequence from Thermus thermophilus HB27. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:AKG, CU
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HOSA_THET2 Catalyzes the aldol-type condensation of 2-oxoglutarate with acetyl-CoA to yield homocitrate (PubMed:19996101, PubMed:12095615). Carries out the first step of the alpha-aminoadipate (AAA) lysine biosynthesis pathway (PubMed:9868782). To a lesser extent, can also use oxaloacetate in place of 2-oxoglutarate, leading to citrate. Does not display 2-isopropylmalate synthase activity since it cannot use 2-oxoisovalerate (PubMed:12095615).[1] [2] [3]

Evolutionary Conservation

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

See Also

References

  1. Wulandari AP, Miyazaki J, Kobashi N, Nishiyama M, Hoshino T, Yamane H. Characterization of bacterial homocitrate synthase involved in lysine biosynthesis. FEBS Lett. 2002 Jul 3;522(1-3):35-40. PMID:12095615 doi:10.1016/s0014-5793(02)02877-6
  2. Okada T, Tomita T, Wulandari AP, Kuzuyama T, Nishiyama M. Mechanism of substrate recognition and insight into feedback inhibition of homocitrate synthase from Thermus thermophilus. J Biol Chem. 2010 Feb 5;285(6):4195-205. Epub 2009 Dec 7. PMID:19996101 doi:10.1074/jbc.M109.086330
  3. Kosuge T, Hoshino T. Lysine is synthesized through the alpha-aminoadipate pathway in Thermus thermophilus. FEMS Microbiol Lett. 1998 Dec 15;169(2):361-7. PMID:9868782 doi:10.1111/j.1574-6968.1998.tb13341.x

Contents


PDB ID 2ztj

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools