2zfh: Difference between revisions

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[[Image:2zfh.png|left|200px]]


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==Crystal structure of putative CutA1 from Homo sapiens at 2.05A resolution==
The line below this paragraph, containing "STRUCTURE_2zfh", creates the "Structure Box" on the page.
<StructureSection load='2zfh' size='340' side='right'caption='[[2zfh]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05&#8491;</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>
{{STRUCTURE_2zfh|  PDB=2zfh  |  SCENE= }}
</table>
== 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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <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>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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/main_output.php?pdb_ID=2zfh ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The 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.


===Crystal structure of putative CutA1 from Homo sapiens at 2.05A resolution===
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<ref>PMID:18453701</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2zfh" style="background-color:#fffaf0;"></div>


==About this Structure==
==See Also==
[[2zfh]] is a 6 chain structure with sequence from [http://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].
*[[CutA1 3D structures|CutA1 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Bagautdinov, B.]]
[[Category: Large Structures]]
[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: Bagautdinov B]]
[[Category: Yutani, K.]]
[[Category: Yutani K]]
[[Category: Human brain]]
[[Category: National project on protein structural and functional analyse]]
[[Category: Nppsfa]]
[[Category: Riken structural genomics/proteomics initiative]]
[[Category: Rsgi]]
[[Category: Structural genomic]]
[[Category: Trimeric structure]]
[[Category: Unknown function]]

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

2zfh is a 6 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.05Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CUTA_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 PubMed

The 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 Also

References

  1. Navaratnam DS, Fernando FS, Priddle JD, Giles K, Clegg SM, Pappin DJ, Craig I, Smith AD. Hydrophobic protein that copurifies with human brain acetylcholinesterase: amino acid sequence, genomic organization, and chromosomal localization. J Neurochem. 2000 May;74(5):2146-53. PMID:10800960
  2. Bagautdinov B, Matsuura Y, Bagautdinova S, Kunishima N, Yutani K. Structure of putative CutA1 from Homo sapiens determined at 2.05 A resolution. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 May 1;64(Pt 5):351-7. Epub, 2008 Apr 30. PMID:18453701 doi:10.1107/S1744309108009846

2zfh, resolution 2.05Å

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