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1goi
From Proteopedia
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| - | [[Image:1goi.gif|left|200px]]<br /><applet load="1goi" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1goi, resolution 1.45Å" /> | ||
| - | '''CRYSTAL STRUCTURE OF THE D140N MUTANT OF CHITINASE B FROM SERRATIA MARCESCENS AT 1.45 A RESOLUTION'''<br /> | ||
| - | == | + | ==Crystal structure of the D140N mutant of chitinase B from Serratia marcescens at 1.45 A resolution== |
| + | <StructureSection load='1goi' size='340' side='right'caption='[[1goi]], [[Resolution|resolution]] 1.45Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1goi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GOI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GOI FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1goi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1goi OCA], [https://pdbe.org/1goi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1goi RCSB], [https://www.ebi.ac.uk/pdbsum/1goi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1goi ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CHIB_SERMA CHIB_SERMA] | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/go/1goi_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=1goi ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The crystal structure of the inactive D140N mutant of Serratia marcescens was refined to 1.45 A resolution. The structure of the mutant was essentially identical to that of the wild type, with the exception of a rotation of Asp142 in the catalytic centre. In the mutant, this residue interacts with the catalytic acid (Glu144) and not with residue 140 as in the wild type. Thus, the 500-fold decrease in activity in the D140N mutant seems to be largely mediated by an effect on Asp142, confirming the crucial role of the latter residue in catalysis. | The crystal structure of the inactive D140N mutant of Serratia marcescens was refined to 1.45 A resolution. The structure of the mutant was essentially identical to that of the wild type, with the exception of a rotation of Asp142 in the catalytic centre. In the mutant, this residue interacts with the catalytic acid (Glu144) and not with residue 140 as in the wild type. Thus, the 500-fold decrease in activity in the D140N mutant seems to be largely mediated by an effect on Asp142, confirming the crucial role of the latter residue in catalysis. | ||
| - | + | Structure of the D140N mutant of chitinase B from Serratia marcescens at 1.45 A resolution.,Kolstad G, Synstad B, Eijsink VG, van Aalten DM Acta Crystallogr D Biol Crystallogr. 2002 Feb;58(Pt 2):377-9. Epub 2002, Jan 24. PMID:11807282<ref>PMID:11807282</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1goi" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Chitinase 3D structures|Chitinase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Serratia marcescens]] | ||
| + | [[Category: Eijsink VGH]] | ||
| + | [[Category: Kolstad G]] | ||
| + | [[Category: Synstad B]] | ||
| + | [[Category: Van Aalten DMF]] | ||
Current revision
Crystal structure of the D140N mutant of chitinase B from Serratia marcescens at 1.45 A resolution
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