4g39: Difference between revisions

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==Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for coordinated electron and proton transfer==
==Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for coordinated electron and proton transfer==
<StructureSection load='4g39' size='340' side='right' caption='[[4g39]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='4g39' size='340' side='right'caption='[[4g39]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4g39]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G39 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G39 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4g39]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G39 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G39 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=SRM:SIROHEME'>SRM</scene></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]] 2.4&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1aop|1aop]], [[4g38|4g38]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SRM:SIROHEME'>SRM</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b2763, cysI, JW2733 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=4g39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g39 OCA], [https://pdbe.org/4g39 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g39 RCSB], [https://www.ebi.ac.uk/pdbsum/4g39 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g39 ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Sulfite_reductase_(NADPH) Sulfite reductase (NADPH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.2 1.8.1.2] </span></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=4g39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g39 OCA], [http://pdbe.org/4g39 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4g39 RCSB], [http://www.ebi.ac.uk/pdbsum/4g39 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4g39 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CYSI_ECOLI CYSI_ECOLI]] Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate.[HAMAP-Rule:MF_01540]  
[https://www.uniprot.org/uniprot/CYSI_ECOLI CYSI_ECOLI] Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate.[HAMAP-Rule:MF_01540]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Ecoli]]
[[Category: Escherichia coli K-12]]
[[Category: Smith, K W]]
[[Category: Large Structures]]
[[Category: Stroupe, M E]]
[[Category: Smith KW]]
[[Category: Oxidoreductase]]
[[Category: Stroupe ME]]
[[Category: Snirr]]
[[Category: Sulfite reductase flavoprotein]]