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1m1m

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{{Seed}}
 
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[[Image:1m1m.png|left|200px]]
 
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==X-RAY CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS BETA-KETOACYL-ACYL CARRIER PROTEIN SYNTHASE III (MTFABH)==
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The line below this paragraph, containing "STRUCTURE_1m1m", creates the "Structure Box" on the page.
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<StructureSection load='1m1m' size='340' side='right'caption='[[1m1m]], [[Resolution|resolution]] 2.70&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'>[[1m1m]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M1M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M1M 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]] 2.7&#8491;</td></tr>
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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=1m1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m1m OCA], [https://pdbe.org/1m1m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m1m RCSB], [https://www.ebi.ac.uk/pdbsum/1m1m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m1m ProSAT]</span></td></tr>
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{{STRUCTURE_1m1m| PDB=1m1m | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FABH_MYCTU FABH_MYCTU] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for long chain acyl-CoA such as myristoyl-CoA. Does not use acyl-CoA as primer. Its substrate specificity determines the biosynthesis of mycolic acid fatty acid chain, which is characteristic of mycobacterial cell wall.<ref>PMID:10840036</ref>
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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/m1/1m1m_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=1m1m ConSurf].
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<div style="clear:both"></div>
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===X-RAY CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS BETA-KETOACYL-ACYL CARRIER PROTEIN SYNTHASE III (MTFABH)===
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==See Also==
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*[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]]
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== References ==
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<references/>
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The line below this paragraph, {{ABSTRACT_PUBMED_16040614}}, adds the Publication Abstract to the page
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__TOC__
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(as it appears on PubMed at http://www.pubmed.gov), where 16040614 is the PubMed ID number.
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</StructureSection>
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[[Category: Large Structures]]
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{{ABSTRACT_PUBMED_16040614}}
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==About this Structure==
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1M1M is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M1M OCA].
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==Reference==
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Probing the mechanism of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III mtFabH: factors influencing catalysis and substrate specificity., Brown AK, Sridharan S, Kremer L, Lindenberg S, Dover LG, Sacchettini JC, Besra GS, J Biol Chem. 2005 Sep 16;280(37):32539-47. Epub 2005 Jul 22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16040614 16040614]
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[[Category: Beta-ketoacyl-acyl-carrier-protein synthase I]]
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[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
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[[Category: Sacchettini, J C.]]
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[[Category: Sacchettini JC]]
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[[Category: Sridharan, S.]]
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[[Category: Sridharan S]]
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[[Category: TBSGC, TB Structural Genomics Consortium.]]
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[[Category: 3-oxoacyl-acyl carrier protein synthase iii]]
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[[Category: Alpha-beta-alpha-beta-alpha]]
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[[Category: Condensing enzyme]]
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[[Category: Mtfabh]]
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[[Category: Protein structure initiative]]
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[[Category: Psi]]
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[[Category: Structural genomic]]
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[[Category: Tb structural genomics consortium]]
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[[Category: Tbsgc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Nov 16 18:01:13 2008''
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Current revision

X-RAY CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS BETA-KETOACYL-ACYL CARRIER PROTEIN SYNTHASE III (MTFABH)

PDB ID 1m1m

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