2zfh: Difference between revisions
No edit summary |
No edit summary |
||
| (3 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Crystal structure of putative CutA1 from Homo sapiens at 2.05A resolution== | ==Crystal structure of putative CutA1 from Homo sapiens at 2.05A resolution== | ||
<StructureSection load='2zfh' size='340' side='right' caption='[[2zfh]], [[Resolution|resolution]] 2.05Å' scene=''> | <StructureSection load='2zfh' size='340' side='right'caption='[[2zfh]], [[Resolution|resolution]] 2.05Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2zfh]] is a 6 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2zfh]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZFH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZFH FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05Å</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=2zfh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zfh OCA], [https://pdbe.org/2zfh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zfh RCSB], [https://www.ebi.ac.uk/pdbsum/2zfh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zfh ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/CUTA_HUMAN CUTA_HUMAN] May form part of a complex of membrane proteins attached to acetylcholinesterase (AChE).<ref>PMID:10800960</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/zf/2zfh_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zf/2zfh_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</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/ | </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=2zfh ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 27: | Line 27: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2zfh" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[CutA1 3D structures|CutA1 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 32: | Line 36: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Bagautdinov B]] | ||
[[Category: Yutani | [[Category: Yutani K]] | ||
Latest revision as of 16:35, 1 November 2023
Crystal structure of putative CutA1 from Homo sapiens at 2.05A resolutionCrystal structure of putative CutA1 from Homo sapiens at 2.05A resolution
Structural highlights
FunctionCUTA_HUMAN May form part of a complex of membrane proteins attached to acetylcholinesterase (AChE).[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 PubMedThe structure of human brain CutA1 (HsCutA1) has been determined using diffraction data to 2.05 A resolution. HsCutA1 has been implicated in the anchoring of acetylcholinesterase in neuronal cell membranes, while its bacterial homologue Escherichia coli CutA1 is involved in copper tolerance. Additionally, the structure of HsCutA1 bears similarity to that of the signal transduction protein PII, which is involved in regulation of nitrogen metabolism. Although several crystal structures of CutA1 from various sources with different rotation angles and degrees of interaction between trimer interfaces have been reported, the specific functional role of CutA1 is still unclear. In this study, the X-ray structure of HsCutA1 was determined in space group P2(1)2(1)2(1), with unit-cell parameters a = 68.69, b = 88.84, c = 125.33 A and six molecules per asymmetric unit. HsCutA1 is a trimeric molecule with intertwined antiparallel beta-strands; each subunit has a molecular weight of 14.6 kDa and contains 135 amino-acid residues. In order to obtain clues to the possible function of HsCutA1, its crystal structure was compared with those of other CutA1 and PII proteins. Structure of putative CutA1 from Homo sapiens determined at 2.05 A resolution.,Bagautdinov B, Matsuura Y, Bagautdinova S, Kunishima N, Yutani K Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 May 1;64(Pt 5):351-7. Epub, 2008 Apr 30. PMID:18453701[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||