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| | <StructureSection load='1zyp' size='340' side='right'caption='[[1zyp]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='1zyp' size='340' side='right'caption='[[1zyp]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1zyp]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZYP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZYP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1zyp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZYP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZYP FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hyu|1hyu]], [[1zyn|1zyn]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</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=1zyp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zyp OCA], [http://pdbe.org/1zyp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zyp RCSB], [http://www.ebi.ac.uk/pdbsum/1zyp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1zyp 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=1zyp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zyp OCA], [https://pdbe.org/1zyp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zyp RCSB], [https://www.ebi.ac.uk/pdbsum/1zyp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zyp ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/AHPF_SALTY AHPF_SALTY]] Serves to protect the cell against DNA damage by alkyl hydroperoxides. It can use either NADH or NADPH as electron donor for direct reduction of redox dyes or of alkyl hydroperoxides when combined with the AhpC protein. | + | [https://www.uniprot.org/uniprot/AHPF_SALTY AHPF_SALTY] Serves to protect the cell against DNA damage by alkyl hydroperoxides. It can use either NADH or NADPH as electron donor for direct reduction of redox dyes or of alkyl hydroperoxides when combined with the AhpC protein. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Jonsson, T J]] | + | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium]] |
| - | [[Category: Karplus, P A]] | + | [[Category: Jonsson TJ]] |
| - | [[Category: Poole, L B]] | + | [[Category: Karplus PA]] |
| - | [[Category: Roberts, B R]] | + | [[Category: Poole LB]] |
| - | [[Category: Wood, Z A]] | + | [[Category: Roberts BR]] |
| - | [[Category: Alkyl hydroperoxide reductase]] | + | [[Category: Wood ZA]] |
| - | [[Category: Disulfide]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Peroxiredoxin]]
| + | |
| - | [[Category: Pka]]
| + | |
| - | [[Category: Radiation damage]]
| + | |
| - | [[Category: Synchrotron radiation]]
| + | |
| - | [[Category: Thiolate]]
| + | |
| - | [[Category: Thioredoxin]]
| + | |
| Structural highlights
Function
AHPF_SALTY Serves to protect the cell against DNA damage by alkyl hydroperoxides. It can use either NADH or NADPH as electron donor for direct reduction of redox dyes or of alkyl hydroperoxides when combined with the AhpC protein.
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 flavoprotein component (AhpF) of Salmonella typhimurium alkyl hydroperoxide reductase contains an N-terminal domain (NTD) with two contiguous thioredoxin folds but only one redox-active disulfide (within the sequence -Cys129-His-Asn-Cys132-). This active site is responsible for mediating the transfer of electrons from the thioredoxin reductase-like segment of AhpF to AhpC, the peroxiredoxin component of the two-protein peroxidase system. The previously reported crystal structure of AhpF possessed a reduced NTD active site, although fully oxidized protein was used for crystallization. To further investigate this active site, we crystallized an isolated recombinant NTD (rNTD); using diffraction data sets collected first at our in-house X-ray source and subsequently at a synchrotron, we showed that the active site disulfide bond (Cys129-Cys132) is oxidized in the native crystals but becomes reduced during synchrotron data collection. The NTD disulfide bond is apparently particularly sensitive to radiation cleavage compared with other protein disulfides. The two data sets provide the first view of an oxidized (disulfide) form of NTD and show that the changes in conformation upon reduction of the disulfide are localized and small. Furthermore, we report the apparent pKa of the active site thiol to be approximately 5.1, a relatively low pKa given its redox potential (approximately 265 mV) compared with most members of the thioredoxin family.
Oxidized and synchrotron cleaved structures of the disulfide redox center in the N-terminal domain of Salmonella typhimurium AhpF.,Roberts BR, Wood ZA, Jonsson TJ, Poole LB, Karplus PA Protein Sci. 2005 Sep;14(9):2414-20. PMID:16131664[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Roberts BR, Wood ZA, Jonsson TJ, Poole LB, Karplus PA. Oxidized and synchrotron cleaved structures of the disulfide redox center in the N-terminal domain of Salmonella typhimurium AhpF. Protein Sci. 2005 Sep;14(9):2414-20. PMID:16131664 doi:14/9/2414
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