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2v9u

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Revision as of 06:42, 5 August 2016

RIM DOMAIN OF MAIN PORIN FROM MYCOBACTERIA SMEGMATIS

Structural highlights

2v9u is a 8 chain structure with sequence from Mycs2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1uun
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

The analysis of natural contact interfaces between protein subunits and between proteins has disclosed some general rules governing their association. We have applied these rules to produce a number of novel assemblies, demonstrating that a given protein can be engineered to form contacts at various points of its surface. Symmetry plays an important role because it defines the multiplicity of a designed contact and therefore the number of required mutations. Some of the proteins needed only a single side-chain alteration in order to associate to a higher-order complex. The mobility of the buried side chains has to be taken into account. Four assemblies have been structurally elucidated. Comparisons between the designed contacts and the results will provide useful guidelines for the development of future architectures.

Designed protein-protein association.,Grueninger D, Treiber N, Ziegler MO, Koetter JW, Schulze MS, Schulz GE Science. 2008 Jan 11;319(5860):206-9. PMID:18187656^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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
↑ Grueninger D, Treiber N, Ziegler MO, Koetter JW, Schulze MS, Schulz GE. Designed protein-protein association. Science. 2008 Jan 11;319(5860):206-9. PMID:18187656 doi:http://dx.doi.org/319/5860/206

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2v9u"

@@ Line 1: / Line 1: @@
 ==RIM DOMAIN OF MAIN PORIN FROM MYCOBACTERIA SMEGMATIS==
 <StructureSection load='2v9u' size='340' side='right' caption='[[2v9u]], [[Resolution|resolution]] 2.59&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2v9u]] is a 8 chain structure with 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=2V9U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V9U FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2v9u]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycs2 Mycs2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V9U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V9U FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1uun|1uun]]</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=2v9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v9u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2v9u RCSB], [http://www.ebi.ac.uk/pdbsum/2v9u PDBsum]</span></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=2v9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v9u OCA], [http://pdbe.org/2v9u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2v9u RCSB], [http://www.ebi.ac.uk/pdbsum/2v9u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2v9u ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/Q9RLP7_MYCSM Q9RLP7_MYCSM]] 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>
+[[http://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]]
@@ Line 16: / Line 17: @@
     <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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=2v9u ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 26: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2v9u" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 33: / Line 35: @@
 __TOC__
 </StructureSection>
-[[Category: Mycobacterium smegmatis]]
+[[Category: Mycs2]]
 [[Category: Grueninger, D]]
 [[Category: Koetter, J W.A]]

2v9u

From Proteopedia

Revision as of 06:42, 5 August 2016

RIM DOMAIN OF MAIN PORIN FROM MYCOBACTERIA SMEGMATIS

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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