4ryt: Difference between revisions

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==Crystal Structure of F222 form of E112A Mutant of Stationary Phase Survival Protein (SurE) from Salmonella typhimurium==
==Crystal Structure of F222 form of E112A Mutant of Stationary Phase Survival Protein (SurE) from Salmonella typhimurium==
<StructureSection load='4ryt' size='340' side='right' caption='[[4ryt]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
<StructureSection load='4ryt' size='340' side='right'caption='[[4ryt]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4ryt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Salty Salty]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RYT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RYT FirstGlance]. <br>
<table><tr><td colspan='2'>[[4ryt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._LT2 Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RYT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RYT FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2v4n|2v4n]], [[2v4o|2v4o]], [[4gad|4gad]], [[4g9o|4g9o]], [[4ryu|4ryu]]</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=4ryt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ryt OCA], [https://pdbe.org/4ryt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ryt RCSB], [https://www.ebi.ac.uk/pdbsum/4ryt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ryt ProSAT]</span></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">surE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=99287 SALTY])</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=4ryt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ryt OCA], [http://pdbe.org/4ryt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ryt RCSB], [http://www.ebi.ac.uk/pdbsum/4ryt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ryt ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/SURE_SALTY SURE_SALTY]] Nucleotidase with a broad substrate specificity as it can dephosphorylate various ribo- and deoxyribonucleoside 5'-monophosphates and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP. Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the preference for short-chain-length substrates (P20-25). Might be involved in the regulation of dNTP and NTP pools, and in the turnover of 3'-mononucleotides produced by numerous intracellular RNases (T1, T2, and F) during the degradation of various RNAs.[HAMAP-Rule:MF_00060]  
[https://www.uniprot.org/uniprot/SURE_SALTY SURE_SALTY] Nucleotidase with a broad substrate specificity as it can dephosphorylate various ribo- and deoxyribonucleoside 5'-monophosphates and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP. Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the preference for short-chain-length substrates (P20-25). Might be involved in the regulation of dNTP and NTP pools, and in the turnover of 3'-mononucleotides produced by numerous intracellular RNases (T1, T2, and F) during the degradation of various RNAs.[HAMAP-Rule:MF_00060]
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Salty]]
[[Category: Large Structures]]
[[Category: Mathiharan, Y K]]
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]]
[[Category: Murthy, M R.N]]
[[Category: Mathiharan YK]]
[[Category: Domain swapping]]
[[Category: Murthy MRN]]
[[Category: Hydrolase]]
[[Category: Phosphatase]]
[[Category: Rossmann fold like]]
[[Category: Stationary phase survival protein]]

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