1nm2
From Proteopedia
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| - | [[Image:1nm2.jpg|left|200px]] | + | [[Image:1nm2.jpg|left|200px]] |
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| - | '''"Malonyl-CoA:ACP Transacylase"''' | + | {{Structure |
| + | |PDB= 1nm2 |SIZE=350|CAPTION= <scene name='initialview01'>1nm2</scene>, resolution 2.00Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene> and <scene name='pdbligand=ACY:ACETIC ACID'>ACY</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= FABD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2 Bacteria]) | ||
| + | }} | ||
| + | |||
| + | '''"Malonyl-CoA:ACP Transacylase"''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1NM2 is a [ | + | 1NM2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteria Bacteria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NM2 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12575934 12575934] |
[[Category: Bacteria]] | [[Category: Bacteria]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: alpha/beta hydrolase-like core]] | [[Category: alpha/beta hydrolase-like core]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:58:35 2008'' |
Revision as of 10:58, 20 March 2008
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| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | FABD (Bacteria) | ||||||
| Activity: | [Acyl-carrier-protein_S-malonyltransferase [Acyl-carrier-protein] S-malonyltransferase], with EC number 2.3.1.39 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
"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. 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 Mar 20 12:58:35 2008
