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| | ==Rv1761c== | | ==Rv1761c== |
| - | <StructureSection load='2k3m' size='340' side='right' caption='[[2k3m]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | + | <StructureSection load='2k3m' size='340' side='right'caption='[[2k3m]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2k3m]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K3M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2K3M FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2k3m]] 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=2K3M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K3M FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MTN:S-[(1-OXYL-2,2,5,5-TETRAMETHYL-2,5-DIHYDRO-1H-PYRROL-3-YL)METHYL]+METHANESULFONOTHIOATE'>MTN</scene></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MT1810, Rv1761c ([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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MTN:S-[(1-OXYL-2,2,5,5-TETRAMETHYL-2,5-DIHYDRO-1H-PYRROL-3-YL)METHYL]+METHANESULFONOTHIOATE'>MTN</scene></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=2k3m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k3m OCA], [http://pdbe.org/2k3m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2k3m RCSB], [http://www.ebi.ac.uk/pdbsum/2k3m 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=2k3m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k3m OCA], [https://pdbe.org/2k3m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k3m RCSB], [https://www.ebi.ac.uk/pdbsum/2k3m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k3m ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/O06796_MYCTU O06796_MYCTU] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cross, T A]] | + | [[Category: Large Structures]] |
| - | [[Category: Lee, S]] | + | [[Category: Mycobacterium tuberculosis]] |
| - | [[Category: Moore, J D]] | + | [[Category: Cross TA]] |
| - | [[Category: Opella, S J]] | + | [[Category: Lee S]] |
| - | [[Category: Page, R C]] | + | [[Category: Moore JD]] |
| - | [[Category: Integral membrane protein]] | + | [[Category: Opella SJ]] |
| - | [[Category: Membrane protein]] | + | [[Category: Page RC]] |
| - | [[Category: Protein]]
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| Structural highlights
Function
O06796_MYCTU
Publication Abstract from PubMed
The structural characterization of small integral membrane proteins pose a significant challenge for structural biology because of the multitude of molecular interactions between the protein and its heterogeneous environment. Here, the three-dimensional backbone structure of Rv1761c from Mycobacterium tuberculosis has been characterized using solution NMR spectroscopy and dodecylphosphocholine (DPC) micelles as a membrane mimetic environment. This 127 residue single transmembrane helix protein has a significant (10 kDa) C-terminal extramembranous domain. Five hundred and ninety distance, backbone dihedral, and orientational restraints were employed resulting in a 1.16 A rmsd backbone structure with a transmembrane domain defined at 0.40 A. The structure determination approach utilized residual dipolar coupling orientation data from partially aligned samples, long-range paramagnetic relaxation enhancement derived distances, and dihedral restraints from chemical shift indices to determine the global fold. This structural model of Rv1761c displays some influences by the membrane mimetic illustrating that the structure of these membrane proteins is dictated by a combination of the amino acid sequence and the protein's environment. These results demonstrate both the efficacy of the structural approach and the necessity to consider the biophysical properties of membrane mimetics when interpreting structural data of integral membrane proteins and, in particular, small integral membrane proteins.
Backbone structure of a small helical integral membrane protein: A unique structural characterization.,Page RC, Lee S, Moore JD, Opella SJ, Cross TA Protein Sci. 2009 Jan;18(1):134-46. doi: 10.1002/pro.24. PMID:19177358[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Page RC, Lee S, Moore JD, Opella SJ, Cross TA. Backbone structure of a small helical integral membrane protein: A unique structural characterization. Protein Sci. 2009 Jan;18(1):134-46. doi: 10.1002/pro.24. PMID:19177358 doi:10.1002/pro.24
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