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1m41

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(New page: 200px<br /><applet load="1m41" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m41, resolution 2.3&Aring;" /> '''Crystal structure of ...)
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[[Image:1m41.gif|left|200px]]<br /><applet load="1m41" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1m41, resolution 2.3&Aring;" />
 
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'''Crystal structure of Escherichia coli alkanesulfonate monooxygenase SsuD at 2.3 A resolution'''<br />
 
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==Overview==
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==Crystal structure of Escherichia coli alkanesulfonate monooxygenase SsuD at 2.3 A resolution==
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The FMNH(2)-dependent alkanesulfonate monooxygenase SsuD catalyzes the, conversion of alkanesulfonates to the corresponding aldehyde and sulfite., The enzyme allows Escherichia coli to use a wide range of alkanesulfonates, as sulfur sources for growth when sulfate or cysteine are not available., The structure of SsuD was solved using the multiwavelength anomalous, dispersion method from only four ordered selenium sites per asymmetric, unit (one site per 20,800 Da). The final model includes 328 of 380 amino, acid residues and was refined to an R-factor of 23.5% (R(free)=27.5%) at, 2.3A resolution. The X-ray crystal structure of SsuD shows a, homotetrameric state for the enzyme, each subunit being composed of a, TIM-barrel fold enlarged by four insertion regions that contribute to, intersubunit interactions. SsuD is structurally related to a bacterial, luciferase and an archaeal coenzyme F(420)-dependent reductase in spite of, a low level of sequence identity with these enzymes. The structural, relationship is not limited to the beta-barrel region; it includes most, but not all extension regions and shows distinct properties for the SsuD, TIM-barrel. A likely substrate-binding site is postulated on the basis of, the SsuD structure presented here, results from earlier biochemical, studies, and structure relatedness to bacterial luciferase. SsuD is, related to other FMNH(2)-dependent monooxygenases that show distant, sequence relationship to luciferase. Thus, the structure reported here, provides a model for enzymes belonging to this family and suggests that, they might all fold as TIM-barrel proteins.
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<StructureSection load='1m41' size='340' side='right'caption='[[1m41]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1m41]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M41 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M41 FirstGlance]. <br>
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1M41 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M41 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]] 2.3&#8491;</td></tr>
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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=1m41 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m41 OCA], [https://pdbe.org/1m41 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m41 RCSB], [https://www.ebi.ac.uk/pdbsum/1m41 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m41 ProSAT]</span></td></tr>
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==Reference==
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</table>
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Crystal structure of Escherichia coli alkanesulfonate monooxygenase SsuD., Eichhorn E, Davey CA, Sargent DF, Leisinger T, Richmond TJ, J Mol Biol. 2002 Nov 29;324(3):457-68. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12445781 12445781]
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== Function ==
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[https://www.uniprot.org/uniprot/SSUD_ECOLI SSUD_ECOLI] Involved in desulfonation of aliphatic sulfonates. Catalyzes the conversion of pentanesulfonic acid to sulfite and pentaldehyde and is able to desulfonate a wide range of sulfonated substrates including C-2 to C-10 unsubstituted linear alkanesulfonates, substituted ethanesulfonic acids and sulfonated buffers.[HAMAP-Rule:MF_01229]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m4/1m41_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1m41 ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Davey, C.A.]]
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[[Category: Davey CA]]
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[[Category: Eichhorn, E.]]
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[[Category: Eichhorn E]]
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[[Category: Leisinger, T.]]
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[[Category: Leisinger T]]
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[[Category: Richmond, T.J.]]
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[[Category: Richmond TJ]]
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[[Category: Sargent, D.F.]]
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[[Category: Sargent DF]]
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[[Category: alkanesulfonate]]
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[[Category: desulfonation]]
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[[Category: fmnh2-dependent monooxygenase]]
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[[Category: monooxygenase]]
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[[Category: oxygenase]]
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[[Category: ssud]]
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[[Category: sulfate starvation]]
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[[Category: sulfur assimilation]]
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[[Category: tim-barrel]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:07:49 2007''
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Current revision

Crystal structure of Escherichia coli alkanesulfonate monooxygenase SsuD at 2.3 A resolution

PDB ID 1m41

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