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| | <StructureSection load='2pqy' size='340' side='right'caption='[[2pqy]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='2pqy' size='340' side='right'caption='[[2pqy]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2pqy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PQY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PQY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2pqy]] is a 1 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=2PQY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PQY FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</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]] 2.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2pqx|2pqx]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rna, rnsA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Enterobacter_ribonuclease Enterobacter ribonuclease], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.6 3.1.27.6] </span></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=2pqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pqy OCA], [https://pdbe.org/2pqy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pqy RCSB], [https://www.ebi.ac.uk/pdbsum/2pqy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pqy ProSAT]</span></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=2pqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pqy OCA], [https://pdbe.org/2pqy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pqy RCSB], [https://www.ebi.ac.uk/pdbsum/2pqy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pqy ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/RNI_ECOLI RNI_ECOLI]] One of the few RNases that cleaves the phosphodiester bond between any two nucleotide. Shows a preference for cytidylic or guanylic acid.
| + | [https://www.uniprot.org/uniprot/RNI_ECOLI RNI_ECOLI] One of the few RNases that cleaves the phosphodiester bond between any two nucleotide. Shows a preference for cytidylic or guanylic acid. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| - | [[Category: Enterobacter ribonuclease]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Loris, R]] | + | [[Category: Loris R]] |
| - | [[Category: Messens, J]] | + | [[Category: Messens J]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Ribonuclease]]
| + | |
| Structural highlights
Function
RNI_ECOLI One of the few RNases that cleaves the phosphodiester bond between any two nucleotide. Shows a preference for cytidylic or guanylic acid.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
One of the last unsolved problems of molecular biology is how the sequential amino acid information leads to a functional protein. Correct disulfide formation within a protein is hereby essential. We present periplasmic ribonuclease I (RNase I) from Escherichia coli as a new endogenous substrate for the study of oxidative protein folding. One of its four disulfides is between nonconsecutive cysteines. In general view, the folding of proteins with nonconsecutive disulfides requires the protein disulfide isomerase DsbC. In contrast, our study with RNase I shows that DsbA is a sufficient catalyst for correct disulfide formation in vivo and in vitro. DsbA is therefore more specific than generally assumed. Further, we show that the redox potential of the periplasm depends on the presence of glutathione and the Dsb proteins to maintain it at-165 mV. We determined the influence of this redox potential on the folding of RNase I. Under the more oxidizing conditions of dsb(-) strains, DsbC becomes necessary to correct non-native disulfides, but it cannot substitute for DsbA. Altogether, DsbA folds a protein with a nonconsecutive disulfide as long as no incorrect disulfides are formed.
The oxidase DsbA folds a protein with a nonconsecutive disulfide.,Messens J, Collet JF, Van Belle K, Brosens E, Loris R, Wyns L J Biol Chem. 2007 Oct 26;282(43):31302-7. Epub 2007 Aug 16. PMID:17702751[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Messens J, Collet JF, Van Belle K, Brosens E, Loris R, Wyns L. The oxidase DsbA folds a protein with a nonconsecutive disulfide. J Biol Chem. 2007 Oct 26;282(43):31302-7. Epub 2007 Aug 16. PMID:17702751 doi:10.1074/jbc.M705236200
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