1i5o: Difference between revisions
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|PDB= 1i5o |SIZE=350|CAPTION= <scene name='initialview01'>1i5o</scene>, resolution 2.8Å | |PDB= 1i5o |SIZE=350|CAPTION= <scene name='initialview01'>1i5o</scene>, resolution 2.8Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=PAL:N-(PHOSPHONACETYL)-L-ASPARTIC+ACID'>PAL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | ||
|ACTIVITY= [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] | |ACTIVITY= <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> | ||
|GENE= PYRB, PYRI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= PYRB, PYRI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[5at1|5at1]], [[6at1|6at1]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i5o OCA], [http://www.ebi.ac.uk/pdbsum/1i5o PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1i5o RCSB]</span> | |||
}} | }} | ||
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[[Category: Stec, B.]] | [[Category: Stec, B.]] | ||
[[Category: Tsuruta, H.]] | [[Category: Tsuruta, H.]] | ||
[[Category: mutant aspartate transcarbamoylase]] | [[Category: mutant aspartate transcarbamoylase]] | ||
[[Category: pala at the regulatory site]] | [[Category: pala at the regulatory site]] | ||
[[Category: t-state]] | [[Category: t-state]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:14:59 2008'' | ||
Revision as of 21:15, 30 March 2008
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| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | PYRB, PYRI (Escherichia coli) | ||||||
| Activity: | Aspartate carbamoyltransferase, with EC number 2.1.3.2 | ||||||
| Related: | 5at1, 6at1
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF MUTANT R105A OF E. COLI ASPARTATE TRANSCARBAMOYLASE
OverviewOverview
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.
About this StructureAbout this Structure
1I5O is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
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
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