2qen: Difference between revisions

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<StructureSection load='2qen' size='340' side='right'caption='[[2qen]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
<StructureSection load='2qen' size='340' side='right'caption='[[2qen]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2qen]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_abyssi Pyrococcus abyssi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QEN OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2QEN FirstGlance]. <br>
<table><tr><td colspan='2'>[[2qen]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_abyssi Pyrococcus abyssi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QEN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QEN FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.25&#8491;</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=2qen FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qen OCA], [http://pdbe.org/2qen PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qen RCSB], [http://www.ebi.ac.uk/pdbsum/2qen PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2qen ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=2qen FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qen OCA], [https://pdbe.org/2qen PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qen RCSB], [https://www.ebi.ac.uk/pdbsum/2qen PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qen ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9V2L3_PYRAB Q9V2L3_PYRAB]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2qen ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2qen ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Several ATPase proteins play essential roles in the initiation of chromosomal DNA replication in archaea. Walker-type ATPases are defined by their conserved Walker A and B motifs, which are associated with nucleotide binding and ATP hydrolysis. A family of 28 ATPase proteins with non-canonical Walker A sequences has been identified by a bioinformatics study of comparative genomics in Pyrococcus genomes. A high-throughput structural study on P. abyssi has been started in order to establish the structure of these proteins. 16 genes have been cloned and characterized. Six out of the seven soluble constructs were purified in Escherichia coli and one of them, PABY2304, has been crystallized. X-ray diffraction data were collected from selenomethionine-derivative crystals using synchrotron radiation. The crystals belong to the orthorhombic space group C2, with unit-cell parameters a = 79.41, b = 48.63, c = 108.77 A, and diffract to beyond 2.6 A resolution.
Cloning, purification and crystallization of a Walker-type Pyrococcus abyssi ATPase family member.,Uhring M, Bey G, Lecompte O, Cavarelli J, Moras D, Poch O Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Oct 1;61(Pt, 10):925-7. Epub 2005 Sep 30. PMID:16511197<ref>PMID:16511197</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2qen" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[ATPase 3D structures|ATPase 3D structures]]
*[[ATPase 3D structures|ATPase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Pyrococcus abyssi]]
[[Category: Pyrococcus abyssi]]
[[Category: Bey, G]]
[[Category: Bey G]]
[[Category: Cavarelli, J]]
[[Category: Cavarelli J]]
[[Category: Lecompte, O]]
[[Category: Lecompte O]]
[[Category: Moras, D]]
[[Category: Moras D]]
[[Category: Poch, O]]
[[Category: Poch O]]
[[Category: Uhring, M]]
[[Category: Uhring M]]
[[Category: Atpase]]
[[Category: Unknown function]]
[[Category: Walker-type]]

Latest revision as of 12:15, 21 February 2024

The walker-type atpase paby2304 of pyrococcus abyssiThe walker-type atpase paby2304 of pyrococcus abyssi

Structural highlights

2qen is a 1 chain structure with sequence from Pyrococcus abyssi. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.25Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q9V2L3_PYRAB

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2qen, resolution 2.25Å

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OCA
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