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==Crystal Structure of E. coli Aspartate Transcarbamoylase K164E/E239K Mutant in an intermediate state==
==Crystal Structure of E. coli Aspartate Transcarbamoylase K164E/E239K Mutant in an intermediate state==
<StructureSection load='4e2f' size='340' side='right' caption='[[4e2f]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='4e2f' size='340' side='right'caption='[[4e2f]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4e2f]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E2F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E2F FirstGlance]. <br>
<table><tr><td colspan='2'>[[4e2f]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E2F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E2F FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><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]] 2.8&#8491;</td></tr>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1za1|1za1]], [[1d09|1d09]]</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><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b4245, JW4204, pyrB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), b4244, JW4203, pyrI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</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=4e2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e2f OCA], [https://pdbe.org/4e2f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e2f RCSB], [https://www.ebi.ac.uk/pdbsum/4e2f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e2f ProSAT]</span></td></tr>
<tr><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>
</table>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4e2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e2f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e2f RCSB], [http://www.ebi.ac.uk/pdbsum/4e2f PDBsum]</span></td></tr>
== Function ==
<table>
[https://www.uniprot.org/uniprot/PYRI_ECOLI PYRI_ECOLI] Involved in allosteric regulation of aspartate carbamoyltransferase.[HAMAP-Rule:MF_00002]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
X-ray crystallography and small-angle X-ray scattering (SAXS) in solution have been used to show that a mutant aspartate transcarbamoylase exists in an intermediate quaternary structure between the canonical T and R structures. Additionally, the SAXS data indicate a pH-dependent structural alteration consistent with either a pH-induced conformational change or a pH-induced alteration in the T to R equilibrium. These data indicate that this mutant is not a model for the R state, as has been proposed, but rather represents the enzyme trapped along the path of the allosteric transition between the T and R states.
 
Trapping and structure determination of an intermediate in the allosteric transition of aspartate transcarbamoylase.,Guo W, West JM, Dutton AS, Tsuruta H, Kantrowitz ER Proc Natl Acad Sci U S A. 2012 Apr 30. PMID:22547808<ref>PMID:22547808</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
==See Also==
</div>
*[[Aspartate carbamoyltransferase 3D structures|Aspartate carbamoyltransferase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Aspartate carbamoyltransferase]]
[[Category: Escherichia coli K-12]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Guo, W.]]
[[Category: Guo W]]
[[Category: Kantrowitz, E R.]]
[[Category: Kantrowitz ER]]
[[Category: Allosteric transition]]
[[Category: Cooperativity]]
[[Category: Intermediate]]
[[Category: Transferase]]
[[Category: Transferase-protein binding complex]]

Latest revision as of 14:01, 1 March 2024

Crystal Structure of E. coli Aspartate Transcarbamoylase K164E/E239K Mutant in an intermediate stateCrystal Structure of E. coli Aspartate Transcarbamoylase K164E/E239K Mutant in an intermediate state

Structural highlights

4e2f is a 12 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PYRI_ECOLI Involved in allosteric regulation of aspartate carbamoyltransferase.[HAMAP-Rule:MF_00002]

See Also

4e2f, resolution 2.80Å

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