Mycobacterium tuberculosis strain π Mycobacterium tuberculosis strain π blueTB molecules protein image

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(gene name ) is involved in the modification of mycolic acids. the Protein belongs to the cyclopropane-fatty-acyl-phospholipid synthase . These enzymes with the activity ( ) catalyse the transfer of a CH3-group from S-adenosylmethionine to an olefinic fatty acid to make it a cyclopropane fatty acid.

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The structural model was obtained from PDB entry , and the description from . Click here to search for at PDB.

protein >

is a peptide of with a and a

Intragenome comparison of identifies many close homologues in , all of which are involved in mycolic acid biosynthesis or modification. In addition there are many proteins with different functions which have lower, but significant homology to . The search for homologues in reveals many similar proteins in other organisms. More functional links are available from the .

dna >

The gene is encoded in a In the M. tuberculosis laboratory strain H37Rv it is a known as which corresponds to gene in the clinical isolate CDC 1551. It can be found on .

 

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On the circular M. tuberculosis chromosome lies at , head to head with umaA1 and close to aceA.

 

ref >

The following tuberculosis-searches could provide additional information for this specific blueTB entry: To obtain a printable version of this blueTB entry click printVersion. Click the reload button to switch back to sectional view.

blueTB molecules are published by Paul Imboden, Dr. PI Bioconsulting. Authorization to photocopy or reproduce this entry for personal use is granted. Copyright @ 2005 Paul Imboden, Dr. PI Bioconsulting. Last modified May 17, 2008 . Disclaimer: blueTB and the author reserves the right to modify and cancel any statement in these documents and regrets, that he cannot accept any responsibility for the consequences of any such changes. to the best of my knowledge all information is correct, but I cannot accept liability for any errors. References for this blueTB entry are:

Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Barrell BG, et al. Nature, 393:537-44 (1998) and the Mycobacterium tuberculosis sequencing project from the Sanger Centre.

Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains. Fleischmann RD, Alland D, Eisen JA, Carpenter L, White O, Peterson J, DeBoy R, Dodson R, Gwinn M, Haft D, Hickey E, Kolonay JF, Nelson WC, Umayam LA, Ermolaeva M, Salzberg SL, Delcher A, Utterback T, Weidman J, Khouri H, Gill J, Mikula A, Bishai W, Jacobs Jr WR Jr, Venter JC, Fraser CM. J Bacteriol. 184:5479-90 (2002) and the Mycobacterium tuberculosis sequencing project from TIGR .

3. Dr. PI's Mtbook, The Mycobacterium tuberculosis genome in a book. Paul Imboden, Dr.PI Bioconsulting. mtbook.drpi.ch/ Release 1.8.0 Jan 2004, which itself is based mainly on reference 1.

Crystal structures of mycolic acid cyclopropane synthases from Mycobacterium tuberculosis. Huang CC, Smith CV, Glickman MS, Jacobs WR Jr, Sacchettini JC. J Biol Chem. 277:11559-11569 (2002)

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