1pg5: Difference between revisions
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==CRYSTAL STRUCTURE OF THE UNLIGATED (T-STATE) ASPARTATE TRANSCARBAMOYLASE FROM THE EXTREMELY THERMOPHILIC ARCHAEON SULFOLOBUS ACIDOCALDARIUS== | ==CRYSTAL STRUCTURE OF THE UNLIGATED (T-STATE) ASPARTATE TRANSCARBAMOYLASE FROM THE EXTREMELY THERMOPHILIC ARCHAEON SULFOLOBUS ACIDOCALDARIUS== | ||
<StructureSection load='1pg5' size='340' side='right' caption='[[1pg5]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='1pg5' size='340' side='right'caption='[[1pg5]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1pg5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_33909 Atcc 33909]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PG5 OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[1pg5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_33909 Atcc 33909]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PG5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1PG5 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[8at1|8at1]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[8at1|8at1]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PYRB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2285 ATCC 33909]), PYRI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2285 ATCC 33909])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PYRB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2285 ATCC 33909]), PYRI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2285 ATCC 33909])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_carbamoyltransferase Aspartate carbamoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.2 2.1.3.2] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_carbamoyltransferase Aspartate carbamoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.2 2.1.3.2] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1pg5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pg5 OCA], [http://pdbe.org/1pg5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pg5 RCSB], [http://www.ebi.ac.uk/pdbsum/1pg5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pg5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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</div> | </div> | ||
<div class="pdbe-citations 1pg5" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1pg5" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Aspartate carbamoyltransferase 3D structures|Aspartate carbamoyltransferase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Aspartate carbamoyltransferase]] | [[Category: Aspartate carbamoyltransferase]] | ||
[[Category: Atcc 33909]] | [[Category: Atcc 33909]] | ||
[[Category: Large Structures]] | |||
[[Category: Beeumen, J J.Van]] | [[Category: Beeumen, J J.Van]] | ||
[[Category: Glansdorff, N]] | [[Category: Glansdorff, N]] | ||
Revision as of 10:29, 9 December 2020
CRYSTAL STRUCTURE OF THE UNLIGATED (T-STATE) ASPARTATE TRANSCARBAMOYLASE FROM THE EXTREMELY THERMOPHILIC ARCHAEON SULFOLOBUS ACIDOCALDARIUSCRYSTAL STRUCTURE OF THE UNLIGATED (T-STATE) ASPARTATE TRANSCARBAMOYLASE FROM THE EXTREMELY THERMOPHILIC ARCHAEON SULFOLOBUS ACIDOCALDARIUS
Structural highlights
Function[PYRI_SULAC] Involved in allosteric regulation of aspartate carbamoyltransferase (By similarity). 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 PubMedAspartate carbamoyltransferase (ATCase) is a model enzyme for understanding allosteric effects. The dodecameric complex exists in two main states (T and R) that differ substantially in their quaternary structure and their affinity for various ligands. Many hypotheses have resulted from the structure of the Escherichia coli ATCase, but so far other crystal structures to test these have been lacking. Here, we present the tertiary and quaternary structure of the T state ATCase of the hyperthermophilic archaeon Sulfolobus acidocaldarius (SaATC(T)), determined by X-ray crystallography to 2.6A resolution. The quaternary structure differs from the E.coli ATCase, by having altered interfaces between the catalytic (C) and regulatory (R) subunits, and the presence of a novel C1-R2 type interface. Conformational differences in the 240 s loop region of the C chain and the C-terminal region of the R chain affect intersubunit and interdomain interfaces implicated previously in the allosteric behavior of E.coli ATCase. The allosteric-zinc binding domain interface is strengthened at the expense of a weakened R1-C4 type interface. The increased hydrophobicity of the C1-R1 type interface may stabilize the quaternary structure. Catalytic trimers of the S.acidocaldarius ATCase are unstable due to a drastic weakening of the C1-C2 interface. The hyperthermophilic ATCase presents an interesting example of how an allosteric enzyme can adapt to higher temperatures. The structural rearrangement of this thermophilic ATCase may well promote its thermal stability at the expense of changes in the allosteric behavior. Crystal structure of T state aspartate carbamoyltransferase of the hyperthermophilic archaeon Sulfolobus acidocaldarius.,De Vos D, Van Petegem F, Remaut H, Legrain C, Glansdorff N, Van Beeumen JJ J Mol Biol. 2004 Jun 11;339(4):887-900. PMID:15165857[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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