1kh1
From Proteopedia
(New page: 200px<br /><applet load="1kh1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kh1, resolution 2.3Å" /> '''Crystal Structure of ...) |
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| - | [[Image:1kh1.gif|left|200px]]<br /><applet load="1kh1" size=" | + | [[Image:1kh1.gif|left|200px]]<br /><applet load="1kh1" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1kh1, resolution 2.3Å" /> | caption="1kh1, resolution 2.3Å" /> | ||
'''Crystal Structure of Thermus thermophilus HB8 Argininosuccinate Synthetase'''<br /> | '''Crystal Structure of Thermus thermophilus HB8 Argininosuccinate Synthetase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Argininosuccinate synthetase catalyzes the ATP-dependent condensation of a | + | Argininosuccinate synthetase catalyzes the ATP-dependent condensation of a citrulline with an aspartate to give argininosuccinate. The three-dimensional structures of the enzyme from Thermus thermophilus HB8 in its free form, complexed with intact ATP, and complexed with an ATP analogue (adenylyl imidodiphosphate) and substrate analogues (arginine and succinate) have been determined at 2.3-, 2.3-, and 1.95-A resolution, respectively. The structure is essentially the same as that of the Escherichia coli argininosuccinate synthetase. The small domain has the same fold as that of a new family of "N-type" ATP pyrophosphatases with the P-loop specific for the pyrophosphate of ATP. However, the enzyme shows the P-loop specific for the gamma-phosphate of ATP. The structure of the complex form is quite similar to that of the native one, indicating that no conformational change occurs upon the binding of ATP and the substrate analogues. ATP and the substrate analogues are bound to the active site with their reaction sites close to one another and located in a geometrical orientation favorable to the catalytic action. The reaction mechanism so far proposed seems to be consistent with the locations of ATP and the substrate analogues. The reaction may proceed without the large conformational change of the enzyme proposed for the catalytic process. |
==About this Structure== | ==About this Structure== | ||
| - | 1KH1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Argininosuccinate_synthase Argininosuccinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.5 6.3.4.5] Full crystallographic information is available from [http:// | + | 1KH1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Argininosuccinate_synthase Argininosuccinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.5 6.3.4.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KH1 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Hirotsu, k.]] | [[Category: Hirotsu, k.]] | ||
[[Category: Nakajima, Y]] | [[Category: Nakajima, Y]] | ||
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: goto, m.]] | [[Category: goto, m.]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:34:02 2008'' |
Revision as of 11:34, 21 February 2008
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Crystal Structure of Thermus thermophilus HB8 Argininosuccinate Synthetase
Overview
Argininosuccinate synthetase catalyzes the ATP-dependent condensation of a citrulline with an aspartate to give argininosuccinate. The three-dimensional structures of the enzyme from Thermus thermophilus HB8 in its free form, complexed with intact ATP, and complexed with an ATP analogue (adenylyl imidodiphosphate) and substrate analogues (arginine and succinate) have been determined at 2.3-, 2.3-, and 1.95-A resolution, respectively. The structure is essentially the same as that of the Escherichia coli argininosuccinate synthetase. The small domain has the same fold as that of a new family of "N-type" ATP pyrophosphatases with the P-loop specific for the pyrophosphate of ATP. However, the enzyme shows the P-loop specific for the gamma-phosphate of ATP. The structure of the complex form is quite similar to that of the native one, indicating that no conformational change occurs upon the binding of ATP and the substrate analogues. ATP and the substrate analogues are bound to the active site with their reaction sites close to one another and located in a geometrical orientation favorable to the catalytic action. The reaction mechanism so far proposed seems to be consistent with the locations of ATP and the substrate analogues. The reaction may proceed without the large conformational change of the enzyme proposed for the catalytic process.
About this Structure
1KH1 is a Single protein structure of sequence from Thermus thermophilus with as ligand. Active as Argininosuccinate synthase, with EC number 6.3.4.5 Full crystallographic information is available from OCA.
Reference
Crystal structure of argininosuccinate synthetase from Thermus thermophilus HB8. Structural basis for the catalytic action., Goto M, Nakajima Y, Hirotsu K, J Biol Chem. 2002 May 3;277(18):15890-6. Epub 2002 Feb 13. PMID:11844799
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