1kph: Difference between revisions

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<StructureSection load='1kph' size='340' side='right'caption='[[1kph]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1kph' size='340' side='right'caption='[[1kph]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1kph]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KPH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1KPH FirstGlance]. <br>
<table><tr><td colspan='2'>[[1kph]] is a 4 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=1KPH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KPH FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=10A:DIDECYL-DIMETHYL-AMMONIUM'>10A</scene>, <scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
</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>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1kp9|1kp9]], [[1kpg|1kpg]], [[1kpi|1kpi]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=10A:DIDECYL-DIMETHYL-AMMONIUM'>10A</scene>, <scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cmaA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</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=1kph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kph OCA], [https://pdbe.org/1kph PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kph RCSB], [https://www.ebi.ac.uk/pdbsum/1kph PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kph ProSAT], [https://www.topsan.org/Proteins/TBSGC/1kph TOPSAN]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cyclopropane-fatty-acyl-phospholipid_synthase Cyclopropane-fatty-acyl-phospholipid synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.79 2.1.1.79] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1kph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kph OCA], [http://pdbe.org/1kph PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kph RCSB], [http://www.ebi.ac.uk/pdbsum/1kph PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kph ProSAT], [http://www.topsan.org/Proteins/TBSGC/1kph TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CMAS1_MYCTU CMAS1_MYCTU]] Catalyzes the conversion of a double bond to a cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence.<ref>PMID:7592990</ref>
[https://www.uniprot.org/uniprot/CMAS1_MYCTU CMAS1_MYCTU] Catalyzes the conversion of a double bond to a cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence.<ref>PMID:7592990</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1kph ConSurf].
</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=1kph ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mycolic acids are major components of the cell wall of Mycobacterium tuberculosis. Several studies indicate that functional groups in the acyl chain of mycolic acids are important for pathogenesis and persistence. There are at least three mycolic acid cyclopropane synthases (PcaA, CmaA1, and CmaA2) that are responsible for these site-specific modifications of mycolic acids. To derive information on the specificity and enzyme mechanism of the family of proteins, the crystal structures of CmaA1, CmaA2, and PcaA were solved to 2-, 2-, and 2.65-A resolution, respectively. All three enzymes have a seven-stranded alpha/beta fold similar to other methyltransferases with the location and interactions with the cofactor S-adenosyl-l-methionine conserved. The structures of the ternary complexes demonstrate the position of the mycolic acid substrate binding site. Close examination of the active site reveals electron density that we believe represents a bicarbonate ion. The structures support the hypothesis that these enzymes catalyze methyl transfer via a carbocation mechanism in which the bicarbonate ion acts as a general base. In addition, comparison of the enzyme structures reveals a possible mechanism for substrate specificity. These structures provide a foundation for rational-drug design, which may lead to the development of new inhibitors effective against persistent bacteria.
Crystal structures of mycolic acid cyclopropane synthases from Mycobacterium tuberculosis.,Huang CC, Smith CV, Glickman MS, Jacobs WR Jr, Sacchettini JC J Biol Chem. 2002 Mar 29;277(13):11559-69. Epub 2001 Dec 26. PMID:11756461<ref>PMID:11756461</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1kph" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Cyclopropane-fatty-acyl-phospholipid synthase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Glickman, M S]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Huang, C C]]
[[Category: Glickman MS]]
[[Category: Jacobs, W R]]
[[Category: Huang C-C]]
[[Category: Sacchettini, J C]]
[[Category: Jacobs Jr WR]]
[[Category: Smith, C V]]
[[Category: Sacchettini JC]]
[[Category: Structural genomic]]
[[Category: Smith CV]]
[[Category: Mixed alpha beta fold]]
[[Category: PSI, Protein structure initiative]]
[[Category: Tbsgc]]
[[Category: Transferase]]

Latest revision as of 10:26, 14 February 2024

Crystal Structure of mycolic acid cyclopropane synthase CmaA1 complexed with SAH and DDDMABCrystal Structure of mycolic acid cyclopropane synthase CmaA1 complexed with SAH and DDDMAB

Structural highlights

1kph is a 4 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 2Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

CMAS1_MYCTU Catalyzes the conversion of a double bond to a cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence.[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. ↑ George KM, Yuan Y, Sherman DR, Barry CE 3rd. The biosynthesis of cyclopropanated mycolic acids in Mycobacterium tuberculosis. Identification and functional analysis of CMAS-2. J Biol Chem. 1995 Nov 10;270(45):27292-8. PMID:7592990

1kph, resolution 2.00Å

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