1kpi
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1kpi |SIZE=350|CAPTION= <scene name='initialview01'>1kpi</scene>, resolution 2.65Å | |PDB= 1kpi |SIZE=350|CAPTION= <scene name='initialview01'>1kpi</scene>, resolution 2.65Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <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> |
|GENE= cmaA2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis]) | |GENE= cmaA2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis]) | ||
| + | |DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam08242 Methyltransf_12], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam02353 CMAS], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=COG2242 CobL]</span> | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kpi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kpi OCA], [http://www.ebi.ac.uk/pdbsum/1kpi PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=1kpi RCSB]</span> | ||
}} | }} | ||
| Line 29: | Line 31: | ||
[[Category: Smith, C V.]] | [[Category: Smith, C V.]] | ||
[[Category: TBSGC, TB Structural Genomics Consortium.]] | [[Category: TBSGC, TB Structural Genomics Consortium.]] | ||
| - | [[Category: 10A]] | ||
| - | [[Category: CO3]] | ||
| - | [[Category: SAH]] | ||
| - | [[Category: SO4]] | ||
[[Category: mixed alpha beta fold]] | [[Category: mixed alpha beta fold]] | ||
[[Category: protein structure initiative]] | [[Category: protein structure initiative]] | ||
| Line 40: | Line 38: | ||
[[Category: tbsgc]] | [[Category: tbsgc]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 05:55:15 2008'' |
Revision as of 03:55, 26 March 2008
| |||||||
| , resolution 2.65Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Gene: | cmaA2 (Mycobacterium tuberculosis) | ||||||
| Activity: | Cyclopropane-fatty-acyl-phospholipid synthase, with EC number 2.1.1.79 | ||||||
| Domains: | Methyltransf_12, CMAS, CobL | ||||||
| Resources: | FirstGlance, OCA, PDBsum, JenaLib, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of mycolic acid cyclopropane synthase CmaA2 complexed with SAH and DDDMAB
Overview
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.
About this Structure
1KPI is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Wed Mar 26 05:55:15 2008
Categories: Cyclopropane-fatty-acyl-phospholipid synthase | Mycobacterium tuberculosis | Single protein | Glickman, M S. | Huang, C C. | Jr., W R.Jacobs. | Sacchettini, J C. | Smith, C V. | TBSGC, TB Structural Genomics Consortium. | Mixed alpha beta fold | Protein structure initiative | Psi | Structural genomic | Tb structural genomics consortium | Tbsgc
