1nm2
From Proteopedia
(New page: 200px<br /><applet load="1nm2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nm2, resolution 2.00Å" /> '''"Malonyl-CoA:ACP Tra...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1nm2.jpg|left|200px]]<br /><applet load="1nm2" size=" | + | [[Image:1nm2.jpg|left|200px]]<br /><applet load="1nm2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1nm2, resolution 2.00Å" /> | caption="1nm2, resolution 2.00Å" /> | ||
'''"Malonyl-CoA:ACP Transacylase"'''<br /> | '''"Malonyl-CoA:ACP Transacylase"'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Malonyl-CoA:ACP transacylase (MAT), the fabD gene product of Streptomyces | + | Malonyl-CoA:ACP transacylase (MAT), the fabD gene product of Streptomyces coelicolor A3(2), participates in both fatty acid and polyketide synthesis pathways, transferring malonyl groups that are used as extender units in chain growth from malonyl-CoA to pathway-specific acyl carrier proteins (ACPs). Here, the 2.0 A structure reveals an invariant arginine bound to an acetate that mimics the malonyl carboxylate and helps define the extender unit binding site. Catalysis may only occur when the oxyanion hole is formed through substrate binding, preventing hydrolysis of the acyl-enzyme intermediate. Macromolecular docking simulations with actinorhodin ACP suggest that the majority of the ACP docking surface is formed by a helical flap. These results should help to engineer polyketide synthases (PKSs) that produce novel polyketides. |
==About this Structure== | ==About this Structure== | ||
| - | 1NM2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteria Bacteria] with NI and ACY as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/[Acyl-carrier-protein]_S-malonyltransferase [Acyl-carrier-protein] S-malonyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.39 2.3.1.39] Full crystallographic information is available from [http:// | + | 1NM2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteria Bacteria] with <scene name='pdbligand=NI:'>NI</scene> and <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/[Acyl-carrier-protein]_S-malonyltransferase [Acyl-carrier-protein] S-malonyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.39 2.3.1.39] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NM2 OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: [Acyl-carrier-protein] S-malonyltransferase]] | [[Category: [Acyl-carrier-protein] S-malonyltransferase]] | ||
| - | [[Category: III, J | + | [[Category: III, J D.O Connell.]] |
| - | [[Category: Keatinge-Clay, A | + | [[Category: Keatinge-Clay, A T.]] |
[[Category: Khosla, C.]] | [[Category: Khosla, C.]] | ||
| - | [[Category: Miercke, L | + | [[Category: Miercke, L J.W.]] |
| - | [[Category: Savage, D | + | [[Category: Savage, D F.]] |
| - | [[Category: Shelat, A | + | [[Category: Shelat, A A.]] |
| - | [[Category: Stroud, R | + | [[Category: Stroud, R M.]] |
[[Category: Tsai, S.]] | [[Category: Tsai, S.]] | ||
[[Category: ACY]] | [[Category: ACY]] | ||
| Line 27: | Line 27: | ||
[[Category: alpha/beta hydrolase-like core]] | [[Category: alpha/beta hydrolase-like core]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:07:31 2008'' |
Revision as of 12:07, 21 February 2008
|
"Malonyl-CoA:ACP Transacylase"
Overview
Malonyl-CoA:ACP transacylase (MAT), the fabD gene product of Streptomyces coelicolor A3(2), participates in both fatty acid and polyketide synthesis pathways, transferring malonyl groups that are used as extender units in chain growth from malonyl-CoA to pathway-specific acyl carrier proteins (ACPs). Here, the 2.0 A structure reveals an invariant arginine bound to an acetate that mimics the malonyl carboxylate and helps define the extender unit binding site. Catalysis may only occur when the oxyanion hole is formed through substrate binding, preventing hydrolysis of the acyl-enzyme intermediate. Macromolecular docking simulations with actinorhodin ACP suggest that the majority of the ACP docking surface is formed by a helical flap. These results should help to engineer polyketide synthases (PKSs) that produce novel polyketides.
About this Structure
1NM2 is a Single protein structure of sequence from Bacteria with and as ligands. Active as [Acyl-carrier-protein_S-malonyltransferase [Acyl-carrier-protein] S-malonyltransferase], with EC number 2.3.1.39 Full crystallographic information is available from OCA.
Reference
Catalysis, specificity, and ACP docking site of Streptomyces coelicolor malonyl-CoA:ACP transacylase., Keatinge-Clay AT, Shelat AA, Savage DF, Tsai SC, Miercke LJ, O'Connell JD 3rd, Khosla C, Stroud RM, Structure. 2003 Feb;11(2):147-54. PMID:12575934[[Category: [Acyl-carrier-protein] S-malonyltransferase]]
Page seeded by OCA on Thu Feb 21 14:07:31 2008
