2fy6

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[[Image:2fy6.gif|left|200px]]
[[Image:2fy6.gif|left|200px]]
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{{Structure
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|PDB= 2fy6 |SIZE=350|CAPTION= <scene name='initialview01'>2fy6</scene>, resolution 1.900&Aring;
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The line below this paragraph, containing "STRUCTURE_2fy6", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptide-methionine-(S)-S-oxide_reductase Peptide-methionine-(S)-S-oxide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.4.11 1.8.4.11] </span>
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|GENE= msrAB, pilB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=65699 Neisseria meningitidis serogroup A])
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|DOMAIN=
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{{STRUCTURE_2fy6| PDB=2fy6 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fy6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fy6 OCA], [http://www.ebi.ac.uk/pdbsum/2fy6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fy6 RCSB]</span>
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'''Structure of the N-terminal domain of Neisseria meningitidis PilB'''
'''Structure of the N-terminal domain of Neisseria meningitidis 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:[http://www.ncbi.nlm.nih.gov/pubmed/16530221 16530221]
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:[http://www.ncbi.nlm.nih.gov/pubmed/16530221 16530221]
[[Category: Neisseria meningitidis serogroup a]]
[[Category: Neisseria meningitidis serogroup a]]
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[[Category: Peptide-methionine-(S)-S-oxide reductase]]
 
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Boschi-Muller, S.]]
[[Category: Boschi-Muller, S.]]
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[[Category: Neiers, F.]]
[[Category: Neiers, F.]]
[[Category: Ranaivoson, F M.]]
[[Category: Ranaivoson, F M.]]
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[[Category: cytochrome maturation protein]]
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[[Category: Cytochrome maturation protein]]
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[[Category: methionine sulfoxide reductase]]
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[[Category: Methionine sulfoxide reductase]]
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[[Category: pilb]]
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[[Category: Pilb]]
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[[Category: thioredoxin]]
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[[Category: Thioredoxin]]
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[[Category: x-ray structure]]
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[[Category: X-ray structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:26:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:09:12 2008''
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Revision as of 01:26, 4 May 2008

Template:STRUCTURE 2fy6

Structure of the N-terminal domain of Neisseria meningitidis PilB


Overview

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 (<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).

About this Structure

2FY6 is a Single protein structure of sequence from Neisseria meningitidis serogroup a. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sun May 4 04:26:25 2008

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