1qe0
From Proteopedia
(New page: 200px<br /><applet load="1qe0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qe0, resolution 2.7Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1qe0.gif|left|200px]]<br /><applet load="1qe0" size=" | + | [[Image:1qe0.gif|left|200px]]<br /><applet load="1qe0" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qe0, resolution 2.7Å" /> | caption="1qe0, resolution 2.7Å" /> | ||
'''CRYSTAL STRUCTURE OF APO S. AUREUS HISTIDYL-TRNA SYNTHETASE'''<br /> | '''CRYSTAL STRUCTURE OF APO S. AUREUS HISTIDYL-TRNA SYNTHETASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the Staphylococcus aureus histidyl-tRNA | + | The crystal structure of the Staphylococcus aureus histidyl-tRNA synthetase apoprotein has been determined at 2.7 A resolution. Several important loops in the active site either become disordered or adopt very different conformations compared to their ligand-bound states. These include the histidine A motif (Arg257-Tyr262) that is essential for substrate recognition, a loop (Gly52-Lys62) that seems to control the communication between the histidine and ATP binding sites, the motif 2 loop (Glu114-Arg120) that binds ATP, and the insertion domain that is likely to bind tRNA. These ligand-induced structural changes are supported by fluorescence experiments, which also suggest highly cooperative dynamics. A dynamic and cooperative active site is most likely necessary for the proper functioning of the histidyl-tRNA synthetase, and suggests a novel mechanism for improving charging fidelity. |
==About this Structure== | ==About this Structure== | ||
| - | 1QE0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Active as [http://en.wikipedia.org/wiki/Histidine--tRNA_ligase Histidine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.21 6.1.1.21] Full crystallographic information is available from [http:// | + | 1QE0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Active as [http://en.wikipedia.org/wiki/Histidine--tRNA_ligase Histidine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.21 6.1.1.21] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QE0 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
| - | [[Category: Abdel-Meguid, S | + | [[Category: Abdel-Meguid, S S.]] |
| - | [[Category: Blackburn, M | + | [[Category: Blackburn, M N.]] |
| - | [[Category: Chohan, I | + | [[Category: Chohan, I K.]] |
[[Category: Hibbs, M.]] | [[Category: Hibbs, M.]] | ||
| - | [[Category: Janson, C | + | [[Category: Janson, C A.]] |
[[Category: Qiu, X.]] | [[Category: Qiu, X.]] | ||
[[Category: beta sheet]] | [[Category: beta sheet]] | ||
[[Category: class ii trna synthetase]] | [[Category: class ii trna synthetase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:38:39 2008'' |
Revision as of 12:38, 21 February 2008
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CRYSTAL STRUCTURE OF APO S. AUREUS HISTIDYL-TRNA SYNTHETASE
Overview
The crystal structure of the Staphylococcus aureus histidyl-tRNA synthetase apoprotein has been determined at 2.7 A resolution. Several important loops in the active site either become disordered or adopt very different conformations compared to their ligand-bound states. These include the histidine A motif (Arg257-Tyr262) that is essential for substrate recognition, a loop (Gly52-Lys62) that seems to control the communication between the histidine and ATP binding sites, the motif 2 loop (Glu114-Arg120) that binds ATP, and the insertion domain that is likely to bind tRNA. These ligand-induced structural changes are supported by fluorescence experiments, which also suggest highly cooperative dynamics. A dynamic and cooperative active site is most likely necessary for the proper functioning of the histidyl-tRNA synthetase, and suggests a novel mechanism for improving charging fidelity.
About this Structure
1QE0 is a Single protein structure of sequence from Staphylococcus aureus. Active as Histidine--tRNA ligase, with EC number 6.1.1.21 Full crystallographic information is available from OCA.
Reference
Cooperative structural dynamics and a novel fidelity mechanism in histidyl-tRNA synthetases., Qiu X, Janson CA, Blackburn MN, Chhohan IK, Hibbs M, Abdel-Meguid SS, Biochemistry. 1999 Sep 21;38(38):12296-304. PMID:10493797
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