1qe0
From Proteopedia
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| - | [[Image:1qe0.gif|left|200px]] | + | [[Image:1qe0.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF APO S. AUREUS HISTIDYL-TRNA SYNTHETASE''' | + | {{Structure |
| + | |PDB= 1qe0 |SIZE=350|CAPTION= <scene name='initialview01'>1qe0</scene>, resolution 2.7Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF APO S. AUREUS HISTIDYL-TRNA SYNTHETASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QE0 is a [ | + | 1QE0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QE0 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10493797 10493797] |
[[Category: Histidine--tRNA ligase]] | [[Category: Histidine--tRNA ligase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: class ii trna synthetase]] | [[Category: class ii trna synthetase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:36:21 2008'' |
Revision as of 11:36, 20 March 2008
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| , resolution 2.7Å | |||||||
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| Activity: | Histidine--tRNA ligase, with EC number 6.1.1.21 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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