1J3N

Crystal Structure of 3-oxoacyl-(acyl-carrier protein) Synthase II from Thermus thermophilus HB8

Summary for 1J3N

• Entry DOI: 10.2210/pdb1j3n/pdb
• Descriptor: 3-oxoacyl-(acyl-carrier protein) synthase II, CITRIC ACID, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: condensing enzymes, fatty acid elongation, acyl-carrier protein (acp), beta-keto-acp synthase (kas), homodimer, structural genomics, riken structural genomics/proteomics initiative, rsgi, transferase
• Biological source: Thermus thermophilus
• Total number of polymer chains: 2
• Total formula weight: 86741.39

Authors

Bagautdinov, B.,Miyano, M.,Tahirov, T.H.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2003-02-10, release date: 2003-03-11, Last modification date: 2023-10-25)

Primary citation

Bagautdinov, B.,Ukita, Y.,Miyano, M.,Kunishima, N.
Structure of 3-oxoacyl-(acyl-carrier protein) synthase II from Thermus thermophilus HB8.
Acta Crystallogr.,Sect.F, 64:358-366, 2008

PubMed Abstract: The beta-ketoacyl-(acyl carrier protein) synthases (beta-keto-ACP synthases; KAS) catalyse the addition of two-carbon units to the growing acyl chain during the elongation phase of fatty-acid synthesis. As key regulators of bacterial fatty-acid synthesis, they are promising targets for the development of new antibacterial agents. The crystal structure of 3-oxoacyl-ACP synthase II from Thermus thermophilus HB8 (TtKAS II) has been solved by molecular replacement and refined at 2.0 A resolution. The crystal is orthorhombic, space group P2(1)2(1)2, with unit-cell parameters a = 72.07, b = 185.57, c = 62.52 A, and contains one homodimer in the asymmetric unit. The subunits adopt the well known alpha-beta-alpha-beta-alpha thiolase fold that is common to ACP synthases. The structural and sequence similarities of TtKAS II to KAS I and KAS II enzymes of known structure from other sources support the hypothesis of comparable enzymatic activity. The dimeric state of TtKAS II is important to create each fatty-acid-binding pocket. Closer examination of KAS structures reveals that compared with other KAS structures in the apo form, the active site of TtKAS II is more accessible because of the ;open' conformation of the Phe396 side chain.

PubMed: 18453702
DOI: 10.1107/S1744309108010336

Experimental method

X-RAY DIFFRACTION (2 Å)