1j3n
From Proteopedia
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'''Crystal Structure of 3-oxoacyl-(acyl-carrier protein) Synthase II from Thermus thermophilus HB8''' | '''Crystal Structure of 3-oxoacyl-(acyl-carrier protein) Synthase II from Thermus thermophilus HB8''' | ||
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| + | ==Overview== | ||
| + | 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. | ||
==About this Structure== | ==About this Structure== | ||
1J3N is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J3N OCA]. | 1J3N is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J3N OCA]. | ||
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| + | ==Reference== | ||
| + | Structure of 3-oxoacyl-(acyl-carrier protein) synthase II from Thermus thermophilus HB8., Bagautdinov B, Ukita Y, Miyano M, Kunishima N, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 May 1;64(Pt, 5):358-66. Epub 2008 Apr 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18453702 18453702] | ||
[[Category: Beta-ketoacyl-acyl-carrier-protein synthase I]] | [[Category: Beta-ketoacyl-acyl-carrier-protein synthase I]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Rsgi]] | [[Category: Rsgi]] | ||
[[Category: Structural genomic]] | [[Category: Structural genomic]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | [[Category: Transferase]] |
| + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu May 22 22:16:13 2008'' | ||
Revision as of 19:16, 22 May 2008
Crystal Structure of 3-oxoacyl-(acyl-carrier protein) Synthase II from Thermus thermophilus HB8
Overview
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.
About this Structure
1J3N is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
Structure of 3-oxoacyl-(acyl-carrier protein) synthase II from Thermus thermophilus HB8., Bagautdinov B, Ukita Y, Miyano M, Kunishima N, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 May 1;64(Pt, 5):358-66. Epub 2008 Apr 30. PMID:18453702 Page seeded by OCA on Thu May 22 22:16:13 2008
Categories: Beta-ketoacyl-acyl-carrier-protein synthase I | Single protein | Thermus thermophilus | Bagautdinov, B. | Miyano, M. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Tahirov, T H. | Condensing enzyme | Fatty acid elongation | Homodimer | Riken structural genomics/proteomics initiative | Rsgi | Structural genomic | Transferase
