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[[Image:1m1m.png|left|200px]]


{{STRUCTURE_1m1m|  PDB=1m1m  |  SCENE=  }}
==X-RAY CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS BETA-KETOACYL-ACYL CARRIER PROTEIN SYNTHASE III (MTFABH)==
 
<StructureSection load='1m1m' size='340' side='right'caption='[[1m1m]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
===X-RAY CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS BETA-KETOACYL-ACYL CARRIER PROTEIN SYNTHASE III (MTFABH)===
== Structural highlights ==
 
<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>
{{ABSTRACT_PUBMED_16040614}}
</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>
 
<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>
==About this Structure==
</table>
[[1m1m]] is a 2 chain structure of [[Acyl carrier protein synthase]] with sequence 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].  
== Function ==
[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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m1/1m1m_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Acyl carrier protein synthase|Acyl carrier protein synthase]]
*[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:016040614</ref><references group="xtra"/>
__TOC__
[[Category: Beta-ketoacyl-acyl-carrier-protein synthase I]]
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Sacchettini, J C.]]
[[Category: Sacchettini JC]]
[[Category: Sridharan, S.]]
[[Category: Sridharan S]]
[[Category: TBSGC, TB Structural Genomics Consortium.]]
[[Category: 3-oxoacyl-acyl carrier protein synthase iii]]
[[Category: Alpha-beta-alpha-beta-alpha]]
[[Category: Condensing enzyme]]
[[Category: Mtfabh]]
[[Category: Protein structure initiative]]
[[Category: Psi]]
[[Category: Structural genomic]]
[[Category: Tb structural genomics consortium]]
[[Category: Tbsgc]]
[[Category: Transferase]]

Latest revision as of 10:38, 14 February 2024

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

Structural highlights

1m1m is a 2 chain structure with sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. Choi KH, Kremer L, Besra GS, Rock CO. Identification and substrate specificity of beta -ketoacyl (acyl carrier protein) synthase III (mtFabH) from Mycobacterium tuberculosis. J Biol Chem. 2000 Sep 8;275(36):28201-7. PMID:10840036 doi:http://dx.doi.org/10.1074/jbc.M003241200

1m1m, resolution 2.70Å

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