1xvw
From Proteopedia
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'''Crystal Structure of AhpE from Mycobacterium tuberculosis, a 1-Cys peroxiredoxin''' | '''Crystal Structure of AhpE from Mycobacterium tuberculosis, a 1-Cys peroxiredoxin''' | ||
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[[Category: TBSGC, TB Structural Genomics Consortium.]] | [[Category: TBSGC, TB Structural Genomics Consortium.]] | ||
[[Category: Yu, M.]] | [[Category: Yu, M.]] | ||
- | [[Category: | + | [[Category: Oxidized cystein sulfenic acid]] |
- | [[Category: | + | [[Category: Protein structure initiative]] |
- | [[Category: | + | [[Category: Psi]] |
- | [[Category: | + | [[Category: Structural genomic]] |
- | [[Category: | + | [[Category: Tb structural genomics consortium]] |
- | [[Category: | + | [[Category: Tbsgc]] |
- | [[Category: | + | [[Category: Thioredoxin fold]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:34:26 2008'' | |
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Revision as of 12:34, 3 May 2008
Crystal Structure of AhpE from Mycobacterium tuberculosis, a 1-Cys peroxiredoxin
Overview
All living systems require protection against the damaging effects of reactive oxygen species. The genome of Mycobacterium tuberculosis, the cause of TB, encodes a number of peroxidases that are thought to be active against organic and inorganic peroxides, and are likely to play a key role in the ability of this organism to survive within the phagosomes of macrophages. The open reading frame Rv2238c in M.tuberculosis encodes a 153-residue protein AhpE, which is a peroxidase of the 1-Cys peroxiredoxin (Prx) family. The crystal structure of AhpE, determined at 1.87 A resolution (R(cryst)=0.179, R(free)=0.210), reveals a compact single-domain protein with a thioredoxin fold. AhpE forms both dimers and octamers; a tightly-associated dimer and a ring-like octamer, generated by crystallographic 4-fold symmetry. In this native structure, the active site Cys45 is in its oxidized, sulfenic acid (S-O-H) state. A second crystal form of AhpE, obtained after soaking in sodium bromide and refined at 1.90 A resolution (R(cryst)=0.242, R(free)=0.286), reveals the reduced structure. In this structure, a conformational change in an external loop, in two of the four molecules in the asymmetric unit, allows Arg116 to stabilise the Cys45 thiolate ion, and concomitantly closes a surface channel. This channel is identified as the likely binding site for a physiological reductant, and the conformational change is inferred to be important for the reaction cycle of AhpE.
About this Structure
1XVW is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
Reference
Crystal Structure of AhpE from Mycobacterium tuberculosis, a 1-Cys peroxiredoxin., Li S, Peterson NA, Kim MY, Kim CY, Hung LW, Yu M, Lekin T, Segelke BW, Lott JS, Baker EN, J Mol Biol. 2005 Mar 4;346(4):1035-46. Epub 2005 Jan 25. PMID:15701515 Page seeded by OCA on Sat May 3 15:34:26 2008
Categories: Mycobacterium tuberculosis | Single protein | Baker, E N. | Hung, L W. | Kim, C Y. | Kim, M Y. | Lekin, T. | Li, S. | Lott, J S. | Peterson, N A. | Segelke, B W. | TBSGC, TB Structural Genomics Consortium. | Yu, M. | Oxidized cystein sulfenic acid | Protein structure initiative | Psi | Structural genomic | Tb structural genomics consortium | Tbsgc | Thioredoxin fold