1i5o
From Proteopedia
(New page: 200px<br /><applet load="1i5o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i5o, resolution 2.8Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1i5o.gif|left|200px]]<br /><applet load="1i5o" size=" | + | [[Image:1i5o.gif|left|200px]]<br /><applet load="1i5o" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1i5o, resolution 2.8Å" /> | caption="1i5o, resolution 2.8Å" /> | ||
'''CRYSTAL STRUCTURE OF MUTANT R105A OF E. COLI ASPARTATE TRANSCARBAMOYLASE'''<br /> | '''CRYSTAL STRUCTURE OF MUTANT R105A OF E. COLI ASPARTATE TRANSCARBAMOYLASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Regulation of protein function, often achieved by allosteric mechanisms, is central to normal physiology and cellular processes. Although numerous | + | 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 Structure== | ==About this Structure== | ||
| - | 1I5O is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ZN and PAL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1I5O is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=PAL:'>PAL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I5O OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Kantrowitz, E | + | [[Category: Kantrowitz, E R.]] |
| - | [[Category: Macol, C | + | [[Category: Macol, C P.]] |
[[Category: Stec, B.]] | [[Category: Stec, B.]] | ||
[[Category: Tsuruta, H.]] | [[Category: Tsuruta, H.]] | ||
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[[Category: t-state]] | [[Category: t-state]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:08:15 2008'' |
Revision as of 11:08, 21 February 2008
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CRYSTAL STRUCTURE OF MUTANT R105A OF E. COLI ASPARTATE TRANSCARBAMOYLASE
Overview
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 Structure
1I5O is a Protein complex structure of sequences from Escherichia coli with and as ligands. Active as Aspartate carbamoyltransferase, with EC number 2.1.3.2 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 13:08:15 2008
