View source for 2l26


==Rv0899 from Mycobacterium tuberculosis contains two separated domains==
<StructureSection load='2l26' size='340' side='right'caption='[[2l26]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2l26]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L26 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L26 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</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=2l26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l26 OCA], [https://pdbe.org/2l26 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l26 RCSB], [https://www.ebi.ac.uk/pdbsum/2l26 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l26 ProSAT]</span></td></tr>
</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;">
== Publication Abstract from PubMed ==
Rv0899 from Mycobacterium tuberculosis belongs to the OmpA (outer membrane protein A) family of outer membrane proteins. It functions as a pore-forming protein; the deletion of this gene impairs the uptake of some water-soluble substances, such as serine, glucose, and glycerol. Rv0899 has also been shown to play a part in low-pH environment adaption, which may play a part in pathogenic mycobacteria overcoming the host's defense mechanisms. Based on many bacterial physiological data and recent structural studies, it was proposed that Rv0899 forms an oligomeric channel to carry out such functions. In this work, biochemical and structural data obtained from solution NMR and EPR spectroscopy indicated that Rv0899 is a monomeric membrane-anchoring protein with two separate domains, rather than an oligomeric pore. Using NMR chemical shift perturbation and isothermal calorimetric titration assays, we show that Rv0899 was able to interact with Zn(2+) ions, which may indicate a role for Rv0899 in the process of Zn(2+) acquisition.

Structural Studies of Mycobacterium tuberculosis Rv0899 Reveal a Monomeric Membrane-Anchoring Protein with Two Separate Domains.,Li J, Shi C, Gao Y, Wu K, Shi P, Lai C, Chen L, Wu F, Tian C J Mol Biol. 2011 Nov 15. PMID:22108166<ref>PMID:22108166</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2l26" style="background-color:#fffaf0;"></div>

==See Also==
*[[Porin 3D structures|Porin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis H37Rv]]
[[Category: Gao Y]]
[[Category: Huang H]]
[[Category: Li J]]
[[Category: Shi C]]
[[Category: Tian C]]
[[Category: Wu K]]