1u9t

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Current revision (08:44, 14 February 2024) (edit) (undo)
 
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<StructureSection load='1u9t' size='340' side='right'caption='[[1u9t]], [[Resolution|resolution]] 2.16&Aring;' scene=''>
<StructureSection load='1u9t' size='340' side='right'caption='[[1u9t]], [[Resolution|resolution]] 2.16&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1u9t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_0157:h7_edl933 Escherichia coli 0157:h7 edl933]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U9T OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1U9T FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1u9t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7_str._EDL933 Escherichia coli O157:H7 str. EDL933]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U9T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U9T FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ChuS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=155864 Escherichia coli 0157:H7 EDL933])</td></tr>
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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]] 2.16&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1u9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u9t OCA], [http://pdbe.org/1u9t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1u9t RCSB], [http://www.ebi.ac.uk/pdbsum/1u9t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1u9t ProSAT], [http://www.topsan.org/Proteins/BSGI/1u9t TOPSAN]</span></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=1u9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u9t OCA], [https://pdbe.org/1u9t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u9t RCSB], [https://www.ebi.ac.uk/pdbsum/1u9t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u9t ProSAT], [https://www.topsan.org/Proteins/BSGI/1u9t TOPSAN]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q8X5N8_ECO57 Q8X5N8_ECO57]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1u9t ConSurf].
</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=1u9t ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Heme oxygenases (HOs) catalyze the oxidation of heme to biliverdin, carbon monoxide (CO), and free iron. Iron acquisition is critical for invading microorganisms to enable survival and growth. Here we report the crystal structure of ChuS, which displays a previously uncharacterized fold and is unique compared with other characterized HOs. Despite only 19% sequence identity between the N- and C-terminal halves, these segments of ChuS represent a structural duplication, with a root-mean-square deviation of 2.1 A between the two repeats. ChuS is capable of using ascorbic acid or cytochrome P450 reductase-NADPH as electron sources for heme oxygenation. CO detection confirmed that ChuS is a HO, and we have identified it in pathogenic Escherichia coli O157:H7. Based on sequence analysis, this HO is present in many bacteria, although not in the E. coli K-12 strain. The N- and C-terminal halves of ChuS are each a functional HO.
 
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Identification of an Escherichia coli O157:H7 heme oxygenase with tandem functional repeats.,Suits MD, Pal GP, Nakatsu K, Matte A, Cygler M, Jia Z Proc Natl Acad Sci U S A. 2005 Nov 22;102(47):16955-60. Epub 2005 Nov 7. PMID:16275907<ref>PMID:16275907</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1u9t" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Escherichia coli 0157:h7 edl933]]
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[[Category: Escherichia coli O157:H7 str. EDL933]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Structural genomic]]
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[[Category: Jia Z]]
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[[Category: Jia, Z]]
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[[Category: Suits MD]]
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[[Category: Suits, M D]]
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[[Category: Bsgi]]
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[[Category: Central beta sheet]]
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[[Category: Flanked by alpha helice]]
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[[Category: Oxidoreductase]]
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[[Category: Structural repeat]]
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Current revision

Crystal Structure Analysis of ChuS, an E. coli Heme Oxygenase

PDB ID 1u9t

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