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| | ==Central B domain of Rv0899 from Mycobacterium tuberculosis== | | ==Central B domain of Rv0899 from Mycobacterium tuberculosis== |
| - | <StructureSection load='2ksm' size='340' side='right' caption='[[2ksm]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2ksm' size='340' side='right'caption='[[2ksm]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ksm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KSM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KSM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ksm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KSM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KSM FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MT0922, MTCY31.27, Rv0899 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ksm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ksm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ksm RCSB], [http://www.ebi.ac.uk/pdbsum/2ksm PDBsum]</span></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=2ksm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ksm OCA], [https://pdbe.org/2ksm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ksm RCSB], [https://www.ebi.ac.uk/pdbsum/2ksm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ksm ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/ARFA_MYCTU ARFA_MYCTU] Probably plays a role in ammonia secretion that neutralizes the medium at pH 5.5, although it does not play a direct role in ammonia transport. The OmpA-like domain (196-326) binds M.tuberculosis peptidoglycan. Overexpression in M.bovis or M.smegmatis gives channels with average conductance value of 1,600 +/- 100 pS, but this may not be physiologically relevant.<ref>PMID:12366842</ref> <ref>PMID:17573469</ref> <ref>PMID:21410778</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 2ksm" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Porin 3D structures|Porin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Mycobacterium tuberculosis]] | | [[Category: Mycobacterium tuberculosis]] |
| - | [[Category: Kolodzik, A.]] | + | [[Category: Kolodzik A]] |
| - | [[Category: Marassi, F M.]] | + | [[Category: Marassi FM]] |
| - | [[Category: Niederweis, M.]] | + | [[Category: Niederweis M]] |
| - | [[Category: Song, H.]] | + | [[Category: Song H]] |
| - | [[Category: Teriete, P.]] | + | [[Category: Teriete P]] |
| - | [[Category: Yao, Y.]] | + | [[Category: Yao Y]] |
| - | [[Category: Yu, J.]] | + | [[Category: Yu J]] |
| - | [[Category: Bon domain]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Ompatb]]
| + | |
| - | [[Category: Transmembrane]]
| + | |
| Structural highlights
Function
ARFA_MYCTU Probably plays a role in ammonia secretion that neutralizes the medium at pH 5.5, although it does not play a direct role in ammonia transport. The OmpA-like domain (196-326) binds M.tuberculosis peptidoglycan. Overexpression in M.bovis or M.smegmatis gives channels with average conductance value of 1,600 +/- 100 pS, but this may not be physiologically relevant.[1] [2] [3]
Publication Abstract from PubMed
The membrane protein Rv0899 (OmpATb) from Mycobacterium tuberculosis, has been proposed to act as an outer membrane porin and to contribute to the bacterium's adaptation to the acidic environment of the phagosome during infection. The gene is restricted to pathogenic mycobacteria and, thus, is an attractive candidate for the development of anti-tuberculosis chemotherapy. The 326-residue protein contains three domains: an N-terminal domain (residues 1-72) that includes a sequence of 20 hydrophobic amino acids required for membrane translocation, a central B domain (residues 73-200) with homology to the conserved putative lipid-binding BON (bacterial OsmY and nodulation) superfamily, and a C domain (residues 201-326) with homology to the OmpA-C-like superfamily of periplasmic peptidoglycan-binding sequences, found in several types of bacterial membrane proteins, including in the C-terminus of the Escherichia coli outer membrane protein OmpA. We have characterized the structure and dynamics of the B and C domains and have determined the three-dimensional structure of the B domain. Rv0899 does not form a transmembrane beta-barrel. Residues 73-326 form a mixed alpha/beta-globular structure, encompassing two independently folded modules corresponding to the B and C domains connected by a flexible linker. The B domain folds with three parallel/antiparallel alpha-helices packed against six parallel/antiparallel beta-strands that form a flat beta-sheet. The core is hydrophobic, while the exterior is polar and predominantly acidic. The structure of a BON homology domain is revealed here for the first time. In light of this unexpected structure, it is hard to reconcile an outer membrane porin activity with the central domain of the protein. The structure of the B domain and the overall architecture of the protein suggest alternative modes of membrane association.
Mycobacterium tuberculosis Rv0899 Adopts a Mixed alpha/beta-Structure and Does Not Form a Transmembrane beta-Barrel.,Teriete P, Yao Y, Kolodzik A, Yu J, Song H, Niederweis M, Marassi FM Biochemistry. 2010 Mar 10. PMID:20199110[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Raynaud C, Papavinasasundaram KG, Speight RA, Springer B, Sander P, Bottger EC, Colston MJ, Draper P. The functions of OmpATb, a pore-forming protein of Mycobacterium tuberculosis. Mol Microbiol. 2002 Oct;46(1):191-201. PMID:12366842
- ↑ Alahari A, Saint N, Campagna S, Molle V, Molle G, Kremer L. The N-terminal domain of OmpATb is required for membrane translocation and pore-forming activity in mycobacteria. J Bacteriol. 2007 Sep;189(17):6351-8. doi: 10.1128/JB.00509-07. Epub 2007 Jun 15. PMID:17573469 doi:http://dx.doi.org/10.1128/JB.00509-07
- ↑ Song H, Huff J, Janik K, Walter K, Keller C, Ehlers S, Bossmann SH, Niederweis M. Expression of the ompATb operon accelerates ammonia secretion and adaptation of Mycobacterium tuberculosis to acidic environments. Mol Microbiol. 2011 May;80(4):900-18. doi: 10.1111/j.1365-2958.2011.07619.x. Epub, 2011 Mar 16. PMID:21410778 doi:http://dx.doi.org/10.1111/j.1365-2958.2011.07619.x
- ↑ Teriete P, Yao Y, Kolodzik A, Yu J, Song H, Niederweis M, Marassi FM. Mycobacterium tuberculosis Rv0899 Adopts a Mixed alpha/beta-Structure and Does Not Form a Transmembrane beta-Barrel. Biochemistry. 2010 Mar 10. PMID:20199110 doi:10.1021/bi100158s
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