1nm2

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{{Seed}}
 
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[[Image:1nm2.png|left|200px]]
 
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==Malonyl-CoA:ACP Transacylase==
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The line below this paragraph, containing "STRUCTURE_1nm2", creates the "Structure Box" on the page.
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<StructureSection load='1nm2' size='340' side='right'caption='[[1nm2]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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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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or leave the SCENE parameter empty for the default display.
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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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<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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{{STRUCTURE_1nm2| PDB=1nm2 | SCENE= }}
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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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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/P72391_STRCH P72391_STRCH]
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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/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 ==
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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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==="Malonyl-CoA:ACP Transacylase"===
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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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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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The line below this paragraph, {{ABSTRACT_PUBMED_12575934}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1nm2" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 12575934 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12575934}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1NM2 is a 1 chain 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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[[Category: Keatinge-Clay AT]]
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[[Category: Khosla C]]
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==Reference==
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[[Category: Miercke LJW]]
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<ref group="xtra">PMID:12575934</ref><references group="xtra"/>
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[[Category: O'Connell III JD]]
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[[Category: Bacteria]]
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[[Category: Savage DF]]
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[[Category: III, J D.O Connell.]]
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[[Category: Shelat AA]]
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[[Category: Keatinge-Clay, A T.]]
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[[Category: Stroud RM]]
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[[Category: Khosla, C.]]
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[[Category: Tsai S]]
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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 Tue Feb 17 17:50:32 2009''
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Current revision

Malonyl-CoA:ACP Transacylase

PDB ID 1nm2

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