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| | <StructureSection load='1nm2' size='340' side='right'caption='[[1nm2]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='1nm2' size='340' side='right'caption='[[1nm2]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1nm2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Strco Strco]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NM2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1NM2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1nm2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor_A3(2) Streptomyces coelicolor A3(2)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NM2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NM2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FABD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=100226 STRCO])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nm2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nm2 OCA], [https://pdbe.org/1nm2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nm2 RCSB], [https://www.ebi.ac.uk/pdbsum/1nm2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nm2 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1nm2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nm2 OCA], [http://pdbe.org/1nm2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nm2 RCSB], [http://www.ebi.ac.uk/pdbsum/1nm2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1nm2 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/P72391_STRCH P72391_STRCH] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Strco]]
| + | [[Category: Keatinge-Clay AT]] |
| - | [[Category: III, J D.O Connell]]
| + | [[Category: Khosla C]] |
| - | [[Category: Keatinge-Clay, A T]] | + | [[Category: Miercke LJW]] |
| - | [[Category: Khosla, C]] | + | [[Category: O'Connell III JD]] |
| - | [[Category: Miercke, L J.W]] | + | [[Category: Savage DF]] |
| - | [[Category: Savage, D F]] | + | [[Category: Shelat AA]] |
| - | [[Category: Shelat, A A]] | + | [[Category: Stroud RM]] |
| - | [[Category: Stroud, R M]] | + | [[Category: Tsai S]] |
| - | [[Category: Tsai, S]] | + | |
| - | [[Category: Acetate bound to active site mimicking a malonyl group]] | + | |
| - | [[Category: Alpha/beta hydrolase-like core]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
P72391_STRCH
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Keatinge-Clay AT, Shelat AA, Savage DF, Tsai SC, Miercke LJ, O'Connell JD 3rd, Khosla C, Stroud RM. Catalysis, specificity, and ACP docking site of Streptomyces coelicolor malonyl-CoA:ACP transacylase. Structure. 2003 Feb;11(2):147-54. PMID:12575934
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