2fy6

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Current revision (13:51, 13 March 2024) (edit) (undo)
 
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<StructureSection load='2fy6' size='340' side='right'caption='[[2fy6]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='2fy6' size='340' side='right'caption='[[2fy6]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2fy6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neima Neima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FY6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FY6 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2fy6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis_Z2491 Neisseria meningitidis Z2491]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FY6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FY6 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">msrAB, pilB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=122587 NEIMA])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peptide-methionine_(S)-S-oxide_reductase Peptide-methionine (S)-S-oxide reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.4.11 1.8.4.11] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fy6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fy6 OCA], [https://pdbe.org/2fy6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fy6 RCSB], [https://www.ebi.ac.uk/pdbsum/2fy6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fy6 ProSAT]</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=2fy6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fy6 OCA], [https://pdbe.org/2fy6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fy6 RCSB], [https://www.ebi.ac.uk/pdbsum/2fy6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fy6 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/MSRAB_NEIMA MSRAB_NEIMA]] Has an important function as a repair enzyme for proteins that have been inactivated by oxidation (By similarity). Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
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[https://www.uniprot.org/uniprot/MSRAB_NEIMA MSRAB_NEIMA] Has an important function as a repair enzyme for proteins that have been inactivated by oxidation (By similarity). Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=2fy6 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=2fy6 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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The secreted form of the PilB protein was recently shown to be bound to the outer membrane of Neisseria gonorrhoeae and proposed to be involved in survival of the pathogen to the host's oxidative burst. PilB is composed of three domains. The central and the C-terminal domains display methionine sulfoxide reductase (Msr) A and B activities respectively, i.e. the ability to reduce specifically the S and the R enantiomers of the sulfoxide function of the methionine sulfoxides, which are easily formed upon oxidation of methionine residues. The N-terminal domain of PilB (Dom1(PILB)) of N.meningitidis, which possesses a CXXC motif, was recently shown to recycle the oxidized forms of the PilB Msr domains in vitro, as the Escherichia coli thioredoxin (Trx) 1 does. The X-ray structure of Dom1(PILB) of N.meningitidis determined here shows a Trx-fold, in agreement with the biochemical properties of Dom1(PILB). However, substantial structural differences with E.coli Trx1 exist. Dom1(PILB) displays more structural homologies with the periplasmic disulfide oxidoreductases involved in cytochrome maturation pathways in bacteria. The active site of the reduced form of Dom1(PILB) reveals a high level of stabilization of the N-terminal catalytic cysteine residue and a hydrophobic environment of the C-terminal recycling cysteine in the CXXC motif, consistent with the pK(app) values measured for Cys67 (&lt;6) and Cys70 (9.3), respectively. Compared to cytochrome maturation disulfide oxidoreductases and to Trx1, one edge of the active site is covered by four additional residues (99)FLHE(102). The putative role of the resulting protuberance is discussed in relation to the disulfide reductase properties of Dom1(PILB).
 
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The X-ray structure of the N-terminal domain of PILB from Neisseria meningitidis reveals a thioredoxin-fold.,Ranaivoson FM, Kauffmann B, Neiers F, Wu J, Boschi-Muller S, Panjikar S, Aubry A, Branlant G, Favier F J Mol Biol. 2006 Apr 28;358(2):443-54. Epub 2006 Feb 28. PMID:16530221<ref>PMID:16530221</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 2fy6" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Neima]]
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[[Category: Neisseria meningitidis Z2491]]
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[[Category: Boschi-Muller, S]]
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[[Category: Boschi-Muller S]]
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[[Category: Branlant, G]]
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[[Category: Branlant G]]
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[[Category: Favier, F]]
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[[Category: Favier F]]
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[[Category: Kauffmann, B]]
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[[Category: Kauffmann B]]
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[[Category: Neiers, F]]
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[[Category: Neiers F]]
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[[Category: Ranaivoson, F M]]
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[[Category: Ranaivoson FM]]
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[[Category: Cytochrome maturation protein]]
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[[Category: Methionine sulfoxide reductase]]
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[[Category: Oxidoreductase]]
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[[Category: Pilb]]
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[[Category: Thioredoxin]]
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Current revision

Structure of the N-terminal domain of Neisseria meningitidis PilB

PDB ID 2fy6

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