1i5o

From Proteopedia

(Difference between revisions)

Revision as of 14:23, 27 October 2021

CRYSTAL STRUCTURE OF MUTANT R105A OF E. COLI ASPARTATE TRANSCARBAMOYLASE

Structural highlights

1i5o is a 4 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	5at1, 6at1
Gene:	PYRB, PYRI ("Bacillus coli" Migula 1895)
Activity:	Aspartate carbamoyltransferase, with EC number 2.1.3.2
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

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

Regulation of protein function, often achieved by allosteric mechanisms, is central to normal physiology and cellular processes. Although numerous models have been proposed to account for the cooperative binding of ligands to allosteric proteins and enzymes, direct structural support has been lacking. Here, we used a combination of X-ray crystallography and small angle X-ray scattering in solution to provide direct structural evidence that the binding of ligand to just one of the six active sites of Escherichia coli aspartate transcarbamoylase induces a concerted structural transition from the T to the R state.

Direct structural evidence for a concerted allosteric transition in Escherichia coli aspartate transcarbamoylase.,Macol CP, Tsuruta H, Stec B, Kantrowitz ER Nat Struct Biol. 2001 May;8(5):423-6. PMID:11323717^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Macol CP, Tsuruta H, Stec B, Kantrowitz ER. Direct structural evidence for a concerted allosteric transition in Escherichia coli aspartate transcarbamoylase. Nat Struct Biol. 2001 May;8(5):423-6. PMID:11323717 doi:http://dx.doi.org/10.1038/87582

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1i5o"

@@ Line 3: / Line 3: @@
 <StructureSection load='1i5o' size='340' side='right'caption='[[1i5o]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1i5o]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I5O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I5O FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1i5o]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I5O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I5O FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PAL:N-(PHOSPHONACETYL)-L-ASPARTIC+ACID'>PAL</scene>, <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"><div style='overflow: auto; max-height: 3em;'>[[5at1|5at1]], [[6at1|6at1]]</div></td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PYRB, PYRI ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Aspartate_carbamoyltransferase Aspartate carbamoyltransferase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=1i5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i5o OCA], [https://pdbe.org/1i5o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i5o RCSB], [https://www.ebi.ac.uk/pdbsum/1i5o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i5o ProSAT]</span></td></tr>
@@ Line 37: / Line 38: @@
 __TOC__
 </StructureSection>
+[[Category: Bacillus coli migula 1895]]
 [[Category: Aspartate carbamoyltransferase]]
 [[Category: Large Structures]]

1i5o

From Proteopedia

Revision as of 14:23, 27 October 2021

CRYSTAL STRUCTURE OF MUTANT R105A OF E. COLI ASPARTATE TRANSCARBAMOYLASE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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