1za1
From Proteopedia
(New page: 200px<br /><applet load="1za1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1za1, resolution 2.20Å" /> '''Structure of wild-ty...) |
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| - | [[Image:1za1.gif|left|200px]]<br /><applet load="1za1" size=" | + | [[Image:1za1.gif|left|200px]]<br /><applet load="1za1" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1za1, resolution 2.20Å" /> | caption="1za1, resolution 2.20Å" /> | ||
'''Structure of wild-type E. coli Aspartate Transcarbamoylase in the presence of CTP at 2.20 A resolution'''<br /> | '''Structure of wild-type E. coli Aspartate Transcarbamoylase in the presence of CTP at 2.20 A resolution'''<br /> | ||
==Overview== | ==Overview== | ||
| - | X-ray structures of aspartate transcarbamoylase in the absence and | + | X-ray structures of aspartate transcarbamoylase in the absence and presence of the first substrate carbamoyl phosphate are reported. These two structures in conjunction with in silico docking experiments provide snapshots of critical events in the function of the enzyme. The ordered substrate binding, observed experimentally, can now be structurally explained by a conformational change induced upon the binding of carbamoyl phosphate. This induced fit dramatically alters the electrostatics of the active site, creating a binding pocket for aspartate. Upon aspartate binding, a further change in electrostatics causes a second induced fit, the domain closure. This domain closure acts as a clamp that both facilitates catalysis by approximation and also initiates the global conformational change that manifests homotropic cooperativity. |
==About this Structure== | ==About this Structure== | ||
| - | 1ZA1 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 CTP 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:// | + | 1ZA1 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=CTP:'>CTP</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=1ZA1 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Cardia, J | + | [[Category: Cardia, J P.]] |
| - | [[Category: Kantrowitz, E | + | [[Category: Kantrowitz, E R.]] |
| - | [[Category: Stieglitz, K | + | [[Category: Stieglitz, K A.]] |
[[Category: Wang, J.]] | [[Category: Wang, J.]] | ||
[[Category: CTP]] | [[Category: CTP]] | ||
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[[Category: x-ray crystallography]] | [[Category: x-ray crystallography]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:13:34 2008'' |
Revision as of 14:13, 21 February 2008
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Structure of wild-type E. coli Aspartate Transcarbamoylase in the presence of CTP at 2.20 A resolution
Overview
X-ray structures of aspartate transcarbamoylase in the absence and presence of the first substrate carbamoyl phosphate are reported. These two structures in conjunction with in silico docking experiments provide snapshots of critical events in the function of the enzyme. The ordered substrate binding, observed experimentally, can now be structurally explained by a conformational change induced upon the binding of carbamoyl phosphate. This induced fit dramatically alters the electrostatics of the active site, creating a binding pocket for aspartate. Upon aspartate binding, a further change in electrostatics causes a second induced fit, the domain closure. This domain closure acts as a clamp that both facilitates catalysis by approximation and also initiates the global conformational change that manifests homotropic cooperativity.
About this Structure
1ZA1 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
Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase., Wang J, Stieglitz KA, Cardia JP, Kantrowitz ER, Proc Natl Acad Sci U S A. 2005 Jun 21;102(25):8881-6. Epub 2005 Jun 10. PMID:15951418
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