1hyu

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(New page: 200px<br /><applet load="1hyu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hyu, resolution 2.00&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1hyu.gif|left|200px]]<br /><applet load="1hyu" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1hyu, resolution 2.00&Aring;" />
 
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'''CRYSTAL STRUCTURE OF INTACT AHPF'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF INTACT AHPF==
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AhpF, a homodimer of 57 kDa subunits, is a flavoenzyme which catalyzes the, NADH-dependent reduction of redox-active disulfide bonds in the peroxidase, AhpC, a member of the recently identified peroxiredoxin class of, antioxidant enzymes. The structure of AhpF from Salmonella typhimurium at, 2.0 A resolution, determined using multiwavelength anomalous dispersion, shows that the C-terminal portion of AhpF (residues 210-521) is, structurally like Escherichia coli thioredoxin reductase. In addition, AhpF has an N-terminal domain (residues 1-196) formed from two contiguous, thioredoxin folds, but containing just a single redox-active disulfide, (Cys129-Cys132). A flexible linker (residues 197-209) connects the, domains, consistent with experiments showing that the N-terminal domain, acts as an appended substrate, first being reduced by the C-terminal, portion of AhpF, and subsequently reducing AhpC. Modeling studies imply, that an intrasubunit electron transfer accounts for the reduction of the, N-terminal domain in dimeric AhpF. Furthermore, comparing the N-terminal, domain with protein disulfide oxidoreductase from Pyrococcus furiosis, we, describe a new class of protein disulfide oxidoreductases based on a novel, mirror-image active site arrangement, with a distinct carboxylate (Glu86), being functionally equivalent to the key acid (Asp26) of E. coli, thioredoxin. A final fortuitous result is that the N-terminal redox center, is reduced and provides a high-resolution view of the thiol-thiolate, hydrogen bond that has been predicted to stabilize the attacking thiolate, in thioredoxin-like proteins.
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<StructureSection load='1hyu' size='340' side='right'caption='[[1hyu]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1hyu]] is a 1 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=1HYU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HYU FirstGlance]. <br>
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1HYU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with SO4, CL and FAD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HYU OCA].
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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]] 2&#8491;</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=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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==Reference==
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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=1hyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hyu OCA], [https://pdbe.org/1hyu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hyu RCSB], [https://www.ebi.ac.uk/pdbsum/1hyu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hyu ProSAT]</span></td></tr>
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Structure of intact AhpF reveals a mirrored thioredoxin-like active site and implies large domain rotations during catalysis., Wood ZA, Poole LB, Karplus PA, Biochemistry. 2001 Apr 3;40(13):3900-11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11300769 11300769]
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</table>
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[[Category: Salmonella typhimurium]]
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== Function ==
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[[Category: Single protein]]
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[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.
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[[Category: Karplus, P.A.]]
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== Evolutionary Conservation ==
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[[Category: Poole, L.B.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Wood, Z.A.]]
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Check<jmol>
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[[Category: CL]]
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<jmolCheckbox>
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[[Category: FAD]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hy/1hyu_consurf.spt"</scriptWhenChecked>
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[[Category: SO4]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: nucleotide binding fold]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: thiol-thiolate hydrogen bond]]
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</jmolCheckbox>
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[[Category: thioredoxin]]
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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=1hyu ConSurf].
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[[Category: thioredoxin reductase]]
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<div style="clear:both"></div>
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__TOC__
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:55:12 2007''
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
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[[Category: Karplus PA]]
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[[Category: Poole LB]]
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[[Category: Wood ZA]]

Current revision

CRYSTAL STRUCTURE OF INTACT AHPF

PDB ID 1hyu

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