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| | <StructureSection load='1ye8' size='340' side='right'caption='[[1ye8]], [[Resolution|resolution]] 1.40Å' scene=''> | | <StructureSection load='1ye8' size='340' side='right'caption='[[1ye8]], [[Resolution|resolution]] 1.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ye8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"aquifex_aeolicus"_huber_and_stetter_2001 "aquifex aeolicus" huber and stetter 2001]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YE8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1YE8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ye8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YE8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YE8 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 1.4Å</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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aq_1292 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=63363 "Aquifex aeolicus" Huber and Stetter 2001])</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=1ye8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ye8 OCA], [https://pdbe.org/1ye8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ye8 RCSB], [https://www.ebi.ac.uk/pdbsum/1ye8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ye8 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1ye8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ye8 OCA], [http://pdbe.org/1ye8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ye8 RCSB], [http://www.ebi.ac.uk/pdbsum/1ye8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ye8 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NTPTH_AQUAE NTPTH_AQUAE]] Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower efficiency. Does not have kinase activity.[HAMAP-Rule:MF_00796]<ref>PMID:14503925</ref> | + | [https://www.uniprot.org/uniprot/NTPTH_AQUAE NTPTH_AQUAE] Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower efficiency. Does not have kinase activity.[HAMAP-Rule:MF_00796]<ref>PMID:14503925</ref> |
| | == 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: Aquifex aeolicus huber and stetter 2001]] | + | [[Category: Aquifex aeolicus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Daumke, O]] | + | [[Category: Daumke O]] |
| - | [[Category: Kaufmann, M]] | + | [[Category: Kaufmann M]] |
| - | [[Category: Klinger, C]] | + | [[Category: Klinger C]] |
| - | [[Category: Rossbach, M]] | + | [[Category: Rossbach M]] |
| - | [[Category: Wittinghofer, A]] | + | [[Category: Wittinghofer A]] |
| - | [[Category: Mixed alpha-beta protein]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
NTPTH_AQUAE Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower efficiency. Does not have kinase activity.[HAMAP-Rule:MF_00796][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
BACKGROUND: aaTHEP1, the gene product of aq_1292 from Aquifex aeolicus, shows sequence homology to proteins from most thermophiles, hyperthermophiles, and higher organisms such as man, mouse, and fly. In contrast, there are almost no homologous proteins in mesophilic unicellular microorganisms. aaTHEP1 is a thermophilic enzyme exhibiting both ATPase and GTPase activity in vitro. Although annotated as a nucleotide kinase, such an activity could not be confirmed for aaTHEP1 experimentally and the in vivo function of aaTHEP1 is still unknown. RESULTS: Here we report the crystal structure of selenomethionine substituted nucleotide-free aaTHEP1 at 1.4 A resolution using a multiple anomalous dispersion phasing protocol. The protein is composed of a single domain that belongs to the family of 3-layer (alpha/beta/alpha)-structures consisting of nine central strands flanked by six helices. The closest structural homologue as determined by DALI is the RecA family. In contrast to the latter proteins, aaTHEP1 possesses an extension of the beta-sheet consisting of four additional beta-strands. CONCLUSION: We conclude that the structure of aaTHEP1 represents a variation of the RecA fold. Although the catalytic function of aaTHEP1 remains unclear, structural details indicate that it does not belong to the group of GTPases, kinases or adenosyltransferases. A mainly positive electrostatic surface indicates that aaTHEP1 might be a DNA/RNA modifying enzyme. The resolved structure of aaTHEP1 can serve as paradigm for the complete THEP1 family.
Crystal structure of THEP1 from the hyperthermophile Aquifex aeolicus: a variation of the RecA fold.,Rossbach M, Daumke O, Klinger C, Wittinghofer A, Kaufmann M BMC Struct Biol. 2005 Mar 20;5:7. PMID:15777481[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Klinger C, Rossbach M, Howe R, Kaufmann M. Thermophile-specific proteins: the gene product of aq_1292 from Aquifex aeolicus is an NTPase. BMC Biochem. 2003 Sep 23;4:12. PMID:14503925 doi:http://dx.doi.org/10.1186/1471-2091-4-12
- ↑ Rossbach M, Daumke O, Klinger C, Wittinghofer A, Kaufmann M. Crystal structure of THEP1 from the hyperthermophile Aquifex aeolicus: a variation of the RecA fold. BMC Struct Biol. 2005 Mar 20;5:7. PMID:15777481 doi:10.1186/1472-6807-5-7
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