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| | ==The 2.0-Angstrom resolution crystal structure of a survival protein E (SurE) homolog from Pyrobaculum aerophilum== | | ==The 2.0-Angstrom resolution crystal structure of a survival protein E (SurE) homolog from Pyrobaculum aerophilum== |
| - | <StructureSection load='1l5x' size='340' side='right' caption='[[1l5x]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='1l5x' size='340' side='right'caption='[[1l5x]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1l5x]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_51768 Atcc 51768]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L5X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1L5X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1l5x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrobaculum_aerophilum Pyrobaculum aerophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L5X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L5X FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1j9j|1j9j]], [[1ilv|1ilv]], [[1j9l|1j9l]], [[1j9k|1j9k]]</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=1l5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l5x OCA], [https://pdbe.org/1l5x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l5x RCSB], [https://www.ebi.ac.uk/pdbsum/1l5x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l5x ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PAE2908 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=13773 ATCC 51768])</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=1l5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l5x OCA], [http://pdbe.org/1l5x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1l5x RCSB], [http://www.ebi.ac.uk/pdbsum/1l5x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1l5x ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SURE1_PYRAE SURE1_PYRAE]] Nucleotidase that shows the greatest phosphatase activity on purine (deoxy)nucleoside 5'-monophosphates, particularly the substrates 5'-GMP, 5'-AMP and 2'-deoxy-5'-AMP.<ref>PMID:12595266</ref> | + | [https://www.uniprot.org/uniprot/SURE1_PYRAE SURE1_PYRAE] Nucleotidase that shows the greatest phosphatase activity on purine (deoxy)nucleoside 5'-monophosphates, particularly the substrates 5'-GMP, 5'-AMP and 2'-deoxy-5'-AMP.<ref>PMID:12595266</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l5/1l5x_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l5/1l5x_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 51768]] | + | [[Category: Large Structures]] |
| - | [[Category: Clarke, S G]] | + | [[Category: Pyrobaculum aerophilum]] |
| - | [[Category: Eisenberg, D]] | + | [[Category: Clarke SG]] |
| - | [[Category: Katz, J E]] | + | [[Category: Eisenberg D]] |
| - | [[Category: Mura, C]] | + | [[Category: Katz JE]] |
| - | [[Category: Mixed alpha/beta protein]] | + | [[Category: Mura C]] |
| - | [[Category: N-terminal rossmann-fold like]]
| + | |
| - | [[Category: Novel c-terminal domain with beta-hairpin extension]]
| + | |
| - | [[Category: Putative acid phosphatase]]
| + | |
| - | [[Category: Structural genomic]]
| + | |
| - | [[Category: Unknown function]]
| + | |
| Structural highlights
Function
SURE1_PYRAE Nucleotidase that shows the greatest phosphatase activity on purine (deoxy)nucleoside 5'-monophosphates, particularly the substrates 5'-GMP, 5'-AMP and 2'-deoxy-5'-AMP.[1]
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
The survival protein E (SurE) family was discovered by its correlation to stationary phase survival of Escherichia coli and various repair proteins involved in sustaining this and other stress-response phenotypes. In order to better understand this ancient and well-conserved protein family, we have determined the 2.0A resolution crystal structure of SurEalpha from the hyperthermophilic crenarchaeon Pyrobaculum aerophilum (Pae). This first structure of an archaeal SurE reveals significant similarities to and differences from the only other known SurE structure, that from the eubacterium Thermatoga maritima (Tma). Both SurE monomers adopt similar folds; however, unlike the Tma SurE dimer, crystalline Pae SurEalpha is predominantly non-domain swapped. Comparative structural analyses of Tma and Pae SurE suggest conformationally variant regions, such as a hinge loop that may be involved in domain swapping. The putative SurE active site is highly conserved, and implies a model for SurE bound to a potential substrate, guanosine-5'-monophosphate (GMP). Pae SurEalpha has optimal acid phosphatase activity at temperatures above 90 degrees C, and is less specific than Tma SurE in terms of metal ion requirements. Substrate specificity also differs between Pae and Tma SurE, with a more specific recognition of purine nucleotides by the archaeal enzyme. Analyses of the sequences, phylogenetic distribution, and genomic organization of the SurE family reveal examples of genomes encoding multiple surE genes, and suggest that SurE homologs constitute a broad family of enzymes with phosphatase-like activities.
Structure and function of an archaeal homolog of survival protein E (SurEalpha): an acid phosphatase with purine nucleotide specificity.,Mura C, Katz JE, Clarke SG, Eisenberg D J Mol Biol. 2003 Mar 7;326(5):1559-75. PMID:12595266[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mura C, Katz JE, Clarke SG, Eisenberg D. Structure and function of an archaeal homolog of survival protein E (SurEalpha): an acid phosphatase with purine nucleotide specificity. J Mol Biol. 2003 Mar 7;326(5):1559-75. PMID:12595266
- ↑ Mura C, Katz JE, Clarke SG, Eisenberg D. Structure and function of an archaeal homolog of survival protein E (SurEalpha): an acid phosphatase with purine nucleotide specificity. J Mol Biol. 2003 Mar 7;326(5):1559-75. PMID:12595266
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