2i4a: Difference between revisions
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==Crystal structure of thioredoxin from the acidophile Acetobacter aceti== | |||
<StructureSection load='2i4a' size='340' side='right'caption='[[2i4a]], [[Resolution|resolution]] 1.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2i4a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acetobacter_aceti Acetobacter aceti]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I4A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I4A 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]] 1Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</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=2i4a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i4a OCA], [https://pdbe.org/2i4a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i4a RCSB], [https://www.ebi.ac.uk/pdbsum/2i4a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i4a ProSAT]</span></td></tr> | |||
</table> | |||
== 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/i4/2i4a_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=2i4a ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The crystal structure of thioredoxin (AaTrx) from the acetic acid bacterium Acetobacter aceti was determined at 1 A resolution. This is currently the highest resolution crystal structure available for any thioredoxin. Thioredoxins facilitate thiol-disulfide exchange, a process that is expected to be slow at the low pH values encountered in the A. aceti cytoplasm. Despite the apparent need to function at low pH, neither the active site nor the surface charge distribution of AaTrx is notably different from that of Escherichia coli thioredoxin. Apparently the ancestral thioredoxin was sufficiently stable for use in A. aceti or the need to interact with multiple targets constrained the variation of surface residues. The AaTrx structure presented here provides a clear view of all ionizable protein moieties and waters, a first step in understanding how thiol-disulfide exchange might occur in a low pH cytoplasm, and is a basis for biophysical studies of the mechanism of acid-mediated unfolding. The high resolution of this structure should be useful for computational studies of thioredoxin function, protein structure and dynamics, and side-chain ionization. | |||
Atomic-resolution crystal structure of thioredoxin from the acidophilic bacterium Acetobacter aceti.,Starks CM, Francois JA, MacArthur KM, Heard BZ, Kappock TJ Protein Sci. 2007 Jan;16(1):92-8. PMID:17192591<ref>PMID:17192591</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2i4a" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Thioredoxin|Thioredoxin]] | *[[Thioredoxin 3D structures|Thioredoxin 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Acetobacter aceti]] | [[Category: Acetobacter aceti]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Kappock TJ]] | ||
[[Category: | [[Category: Starks CM]] | ||
Latest revision as of 13:05, 30 August 2023
Crystal structure of thioredoxin from the acidophile Acetobacter acetiCrystal structure of thioredoxin from the acidophile Acetobacter aceti
Structural highlights
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 crystal structure of thioredoxin (AaTrx) from the acetic acid bacterium Acetobacter aceti was determined at 1 A resolution. This is currently the highest resolution crystal structure available for any thioredoxin. Thioredoxins facilitate thiol-disulfide exchange, a process that is expected to be slow at the low pH values encountered in the A. aceti cytoplasm. Despite the apparent need to function at low pH, neither the active site nor the surface charge distribution of AaTrx is notably different from that of Escherichia coli thioredoxin. Apparently the ancestral thioredoxin was sufficiently stable for use in A. aceti or the need to interact with multiple targets constrained the variation of surface residues. The AaTrx structure presented here provides a clear view of all ionizable protein moieties and waters, a first step in understanding how thiol-disulfide exchange might occur in a low pH cytoplasm, and is a basis for biophysical studies of the mechanism of acid-mediated unfolding. The high resolution of this structure should be useful for computational studies of thioredoxin function, protein structure and dynamics, and side-chain ionization. Atomic-resolution crystal structure of thioredoxin from the acidophilic bacterium Acetobacter aceti.,Starks CM, Francois JA, MacArthur KM, Heard BZ, Kappock TJ Protein Sci. 2007 Jan;16(1):92-8. PMID:17192591[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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