1nm2

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[[Image:1nm2.png|left|200px]]
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=="Malonyl-CoA:ACP Transacylase"==
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<StructureSection load='1nm2' size='340' side='right' caption='[[1nm2]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1nm2]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NM2 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene><br>
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<tr><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 Streptomyces coelicolor A3(2)])</td></tr>
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<tr><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>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nm2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nm2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1nm2 RCSB], [http://www.ebi.ac.uk/pdbsum/1nm2 PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nm/1nm2_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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{{STRUCTURE_1nm2| PDB=1nm2 | SCENE= }}
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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<ref>PMID:12575934</ref>
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==="Malonyl-CoA:ACP Transacylase"===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_12575934}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[1nm2]] is a 1 chain structure with sequence from [http://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].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:012575934</ref><references group="xtra"/>
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[[Category: III, J D.O Connell.]]
[[Category: III, J D.O Connell.]]
[[Category: Keatinge-Clay, A T.]]
[[Category: Keatinge-Clay, A T.]]

Revision as of 15:58, 28 September 2014

"Malonyl-CoA:ACP Transacylase"

1nm2, resolution 2.00Å

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OCA

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