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| | {{STRUCTURE_1xvw| PDB=1xvw | SCENE= }} | | {{STRUCTURE_1xvw| PDB=1xvw | SCENE= }} |
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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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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15701515}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15701515 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15701515}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Tbsgc]] | | [[Category: Tbsgc]] |
| | [[Category: Thioredoxin fold]] | | [[Category: Thioredoxin fold]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:34:26 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:22:17 2008'' |
Revision as of 13:22, 27 July 2008
Template:STRUCTURE 1xvw
Crystal Structure of AhpE from Mycobacterium tuberculosis, a 1-Cys peroxiredoxin
Template:ABSTRACT PUBMED 15701515
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 Sun Jul 27 16:22:17 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