1r4v: Difference between revisions
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New page: left|200px<br /><applet load="1r4v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r4v, resolution 1.90Å" /> '''1.9A crystal structu... |
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== | ==1.9A crystal structure of protein AQ328 from Aquifex aeolicus== | ||
The structure of Aq_328, an uncharacterized protein from hyperthermophilic | <StructureSection load='1r4v' size='340' side='right'caption='[[1r4v]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1r4v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus_VF5 Aquifex aeolicus VF5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R4V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R4V FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1r4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r4v OCA], [https://pdbe.org/1r4v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r4v RCSB], [https://www.ebi.ac.uk/pdbsum/1r4v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r4v ProSAT], [https://www.topsan.org/Proteins/MCSG/1r4v TOPSAN]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Y328_AQUAE Y328_AQUAE] | |||
== 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/r4/1r4v_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1r4v ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The structure of Aq_328, an uncharacterized protein from hyperthermophilic bacteria Aquifex aeolicus, has been determined to 1.9 A by using multi-wavelength anomalous diffraction (MAD) phasing. Although the amino acid sequence analysis shows that Aq_328 has no significant similarity to proteins with a known structure and function, the structure comparison by using the Dali server reveals that it: (1) assumes a histone-like fold, and (2) is similar to an ancestral nuclear histone protein (PDB code 1F1E) with z-score 8.1 and RMSD 3.6 A over 124 residues. A sedimentation equilibrium experiment indicates that Aq_328 is a monomer in solution, with an average sedimentation coefficient of 2.4 and an apparent molecular weight of about 20 kDa. The overall architecture of Aq_328 consists of two noncanonical histone domains in tandem repeat within a single chain, and is similar to eukaryotic heterodimer (H2A/H2B and H3/H4) and an archaeal histone heterodimer (HMfA/HMfB). The sequence comparisons between the two histone domains of Aq_328 and six eukaryotic/archaeal histones demonstrate that most of the conserved residues that underlie the Aq_328 architecture are used to build and stabilize the two cross-shaped antiparallel histone domains. The high percentage of salt bridges in the structure could be a factor in the protein's thermostability. The structural similarities to other histone-like proteins, molecular properties, and potential function of Aq_328 are discussed in this paper. | |||
The crystal structure of Aq_328 from the hyperthermophilic bacteria Aquifex aeolicus shows an ancestral histone fold.,Qiu Y, Tereshko V, Kim Y, Zhang R, Collart F, Yousef M, Kossiakoff A, Joachimiak A Proteins. 2006 Jan 1;62(1):8-16. PMID:16287087<ref>PMID:16287087</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: Aquifex aeolicus]] | <div class="pdbe-citations 1r4v" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Collart | <references/> | ||
[[Category: Joachimiak | __TOC__ | ||
[[Category: Kim | </StructureSection> | ||
[[Category: Kossiakoff | [[Category: Aquifex aeolicus VF5]] | ||
[[Category: Large Structures]] | |||
[[Category: Qiu | [[Category: Collart F]] | ||
[[Category: Tereshko | [[Category: Joachimiak A]] | ||
[[Category: Zhang | [[Category: Kim Y]] | ||
[[Category: Kossiakoff A]] | |||
[[Category: Qiu Y]] | |||
[[Category: Tereshko V]] | |||
[[Category: Zhang R]] | |||
Latest revision as of 07:17, 30 October 2024
1.9A crystal structure of protein AQ328 from Aquifex aeolicus
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