1nm2

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[[Image:1nm2.jpg|left|200px]]
 
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{{Structure
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==Malonyl-CoA:ACP Transacylase==
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|PDB= 1nm2 |SIZE=350|CAPTION= <scene name='initialview01'>1nm2</scene>, resolution 2.00&Aring;
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<StructureSection load='1nm2' size='340' side='right'caption='[[1nm2]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>
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<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>
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|ACTIVITY= <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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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|GENE= FABD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2 Bacteria])
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<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>
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|DOMAIN=
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<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>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<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.ebi.ac.uk/pdbsum/1nm2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nm2 RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/P72391_STRCH P72391_STRCH]
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== Evolutionary Conservation ==
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'''"Malonyl-CoA:ACP Transacylase"'''
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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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==Overview==
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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/main_output.php?pdb_ID=1nm2 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 ==
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.
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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==About this Structure==
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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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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].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12575934 12575934]
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[[Category: Bacteria]]
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[[Category: Single protein]]
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[[Category: [Acyl-carrier-protein] S-malonyltransferase]]
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[[Category: III, J D.O Connell.]]
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[[Category: Keatinge-Clay, A T.]]
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[[Category: Khosla, C.]]
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[[Category: Miercke, L J.W.]]
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[[Category: Savage, D F.]]
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[[Category: Shelat, A A.]]
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[[Category: Stroud, R M.]]
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[[Category: Tsai, S.]]
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[[Category: acetate bound to active site mimicking a malonyl group]]
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[[Category: alpha/beta hydrolase-like core]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:32:17 2008''
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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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<div class="pdbe-citations 1nm2" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Keatinge-Clay AT]]
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[[Category: Khosla C]]
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[[Category: Miercke LJW]]
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[[Category: O'Connell III JD]]
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[[Category: Savage DF]]
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[[Category: Shelat AA]]
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[[Category: Stroud RM]]
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[[Category: Tsai S]]

Current revision

Malonyl-CoA:ACP Transacylase

PDB ID 1nm2

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