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| - | [[Image:1uun.jpg|left|200px]] | |
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| - | <!-- | + | ==Main porin from Mycobacterium smegmatis (MspA)== |
| - | The line below this paragraph, containing "STRUCTURE_1uun", creates the "Structure Box" on the page.
| + | <StructureSection load='1uun' size='340' side='right'caption='[[1uun]], [[Resolution|resolution]] 2.50Å' scene=''> |
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | + | <table><tr><td colspan='2'>[[1uun]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis Mycolicibacterium smegmatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UUN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UUN FirstGlance]. <br> |
| - | or leave the SCENE parameter empty for the default display.
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</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=1uun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uun OCA], [https://pdbe.org/1uun PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uun RCSB], [https://www.ebi.ac.uk/pdbsum/1uun PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uun ProSAT]</span></td></tr> |
| - | {{STRUCTURE_1uun| PDB=1uun | SCENE= }}
| + | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/MSPA_MYCS2 MSPA_MYCS2] The major porin in this organism, forms a water-filled channel which favors the permeation of cations, amino acids, iron Fe(3+) and less efficiently phosphate. Does not transport Fe-ExoMS, the predominant siderophore. Plays a role in transport of beta-lactamase and hydrophilic fluoroquinolone antibiotics such as norfloxacin as well as chloramphenicol. There are about 2400 porins in wild-type, 800 in an mspA deletion and 150 in a double mspA-mspC deletion. Different conductance values with maxima at 2.3 and 4.6 nanosiemens might be caused by a simultaneous reconstitution of MspA channels into the membrane or by the existence of different MspA conformations.<ref>PMID:10476028</ref> <ref>PMID:16238622</ref> <ref>PMID:17209034</ref> <ref>PMID:18559650</ref> <ref>PMID:20952578</ref> |
| | + | == Evolutionary Conservation == |
| | + | [[Image:Consurf_key_small.gif|200px|right]] |
| | + | Check<jmol> |
| | + | <jmolCheckbox> |
| | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uu/1uun_consurf.spt"</scriptWhenChecked> |
| | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | + | <text>to colour the structure by Evolutionary Conservation</text> |
| | + | </jmolCheckbox> |
| | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1uun ConSurf]. |
| | + | <div style="clear:both"></div> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == Publication Abstract from PubMed == |
| | + | Mycobacteria have low-permeability outer membranes that render them resistant to most antibiotics. Hydrophilic nutrients can enter by way of transmembrane-channel proteins called porins. An x-ray analysis of the main porin from Mycobacterium smegmatis, MspA, revealed a homooctameric goblet-like conformation with a single central channel. This is the first structure of a mycobacterial outer-membrane protein. No structure-related protein was found in the Protein Data Bank. MspA contains two consecutive beta barrels with nonpolar outer surfaces that form a ribbon around the porin, which is too narrow to fit the thickness of the mycobacterial outer membrane in contemporary models. |
| | | | |
| - | '''MAIN PORIN FROM MYCOBACTERIA SMEGMATIS (MSPA)'''
| + | The structure of a mycobacterial outer-membrane channel.,Faller M, Niederweis M, Schulz GE Science. 2004 Feb 20;303(5661):1189-92. PMID:14976314<ref>PMID:14976314</ref> |
| - | | + | |
| - | | + | |
| - | ==Overview==
| + | |
| - | Mycobacteria have low-permeability outer membranes that render them resistant to most antibiotics. Hydrophilic nutrients can enter by way of transmembrane-channel proteins called porins. An x-ray analysis of the main porin from Mycobacterium smegmatis, MspA, revealed a homooctameric goblet-like conformation with a single central channel. This is the first structure of a mycobacterial outer-membrane protein. No structure-related protein was found in the Protein Data Bank. MspA contains two consecutive beta barrels with nonpolar outer surfaces that form a ribbon around the porin, which is too narrow to fit the thickness of the mycobacterial outer membrane in contemporary models.
| + | |
| | | | |
| - | ==About this Structure==
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | 1UUN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_smegmatis Mycobacterium smegmatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UUN OCA].
| + | </div> |
| | + | <div class="pdbe-citations 1uun" style="background-color:#fffaf0;"></div> |
| | | | |
| - | ==Reference== | + | ==See Also== |
| - | The structure of a mycobacterial outer-membrane channel., Faller M, Niederweis M, Schulz GE, Science. 2004 Feb 20;303(5661):1189-92. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14976314 14976314]
| + | *[[Porin 3D structures|Porin 3D structures]] |
| - | [[Category: Mycobacterium smegmatis]] | + | == References == |
| - | [[Category: Single protein]] | + | <references/> |
| - | [[Category: Faller, M.]] | + | __TOC__ |
| - | [[Category: Niederweis, M.]] | + | </StructureSection> |
| - | [[Category: Schulz, G E.]] | + | [[Category: Large Structures]] |
| - | [[Category: Mycobacteria]]
| + | [[Category: Mycolicibacterium smegmatis]] |
| - | [[Category: Porin]]
| + | [[Category: Faller M]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:43:03 2008''
| + | [[Category: Niederweis M]] |
| | + | [[Category: Schulz GE]] |
| Structural highlights
Function
MSPA_MYCS2 The major porin in this organism, forms a water-filled channel which favors the permeation of cations, amino acids, iron Fe(3+) and less efficiently phosphate. Does not transport Fe-ExoMS, the predominant siderophore. Plays a role in transport of beta-lactamase and hydrophilic fluoroquinolone antibiotics such as norfloxacin as well as chloramphenicol. There are about 2400 porins in wild-type, 800 in an mspA deletion and 150 in a double mspA-mspC deletion. Different conductance values with maxima at 2.3 and 4.6 nanosiemens might be caused by a simultaneous reconstitution of MspA channels into the membrane or by the existence of different MspA conformations.[1] [2] [3] [4] [5]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Mycobacteria have low-permeability outer membranes that render them resistant to most antibiotics. Hydrophilic nutrients can enter by way of transmembrane-channel proteins called porins. An x-ray analysis of the main porin from Mycobacterium smegmatis, MspA, revealed a homooctameric goblet-like conformation with a single central channel. This is the first structure of a mycobacterial outer-membrane protein. No structure-related protein was found in the Protein Data Bank. MspA contains two consecutive beta barrels with nonpolar outer surfaces that form a ribbon around the porin, which is too narrow to fit the thickness of the mycobacterial outer membrane in contemporary models.
The structure of a mycobacterial outer-membrane channel.,Faller M, Niederweis M, Schulz GE Science. 2004 Feb 20;303(5661):1189-92. PMID:14976314[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Niederweis M, Ehrt S, Heinz C, Klocker U, Karosi S, Swiderek KM, Riley LW, Benz R. Cloning of the mspA gene encoding a porin from Mycobacterium smegmatis. Mol Microbiol. 1999 Sep;33(5):933-45. PMID:10476028
- ↑ Stephan J, Bender J, Wolschendorf F, Hoffmann C, Roth E, Mailander C, Engelhardt H, Niederweis M. The growth rate of Mycobacterium smegmatis depends on sufficient porin-mediated influx of nutrients. Mol Microbiol. 2005 Nov;58(3):714-30. PMID:16238622 doi:http://dx.doi.org/10.1111/j.1365-2958.2005.04878.x
- ↑ Wolschendorf F, Mahfoud M, Niederweis M. Porins are required for uptake of phosphates by Mycobacterium smegmatis. J Bacteriol. 2007 Mar;189(6):2435-42. Epub 2007 Jan 5. PMID:17209034 doi:http://dx.doi.org/10.1128/JB.01600-06
- ↑ Danilchanka O, Pavlenok M, Niederweis M. Role of porins for uptake of antibiotics by Mycobacterium smegmatis. Antimicrob Agents Chemother. 2008 Sep;52(9):3127-34. doi: 10.1128/AAC.00239-08., Epub 2008 Jun 16. PMID:18559650 doi:http://dx.doi.org/10.1128/AAC.00239-08
- ↑ Jones CM, Niederweis M. Role of porins in iron uptake by Mycobacterium smegmatis. J Bacteriol. 2010 Dec;192(24):6411-7. doi: 10.1128/JB.00986-10. Epub 2010 Oct 15. PMID:20952578 doi:http://dx.doi.org/10.1128/JB.00986-10
- ↑ Faller M, Niederweis M, Schulz GE. The structure of a mycobacterial outer-membrane channel. Science. 2004 Feb 20;303(5661):1189-92. PMID:14976314 doi:10.1126/science.1094114
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