1set
From Proteopedia
(New page: 200px<br /> <applet load="1set" size="450" color="white" frame="true" align="right" spinBox="true" caption="1set, resolution 2.55Å" /> '''CRYSTAL STRUCTURES ...) |
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caption="1set, resolution 2.55Å" /> | caption="1set, resolution 2.55Å" /> | ||
'''CRYSTAL STRUCTURES AT 2.5 ANGSTROMS RESOLUTION OF SERYL-TRNA SYNTHETASE COMPLEXED WITH TWO DIFFERENT ANALOGUES OF SERYL-ADENYLATE'''<br /> | '''CRYSTAL STRUCTURES AT 2.5 ANGSTROMS RESOLUTION OF SERYL-TRNA SYNTHETASE COMPLEXED WITH TWO DIFFERENT ANALOGUES OF SERYL-ADENYLATE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1SET 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 SSA as [http://en.wikipedia.org/wiki/ligand ligand]. The following page contains interesting information on the relation of 1SET with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb16_1.html Aminoacyl-tRNA Synthetases]]. Active as [http://en.wikipedia.org/wiki/Serine--tRNA_ligase Serine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.11 6.1.1.11] Full crystallographic information is available from [http:// | + | 1SET 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=SSA:'>SSA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. The following page contains interesting information on the relation of 1SET with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb16_1.html Aminoacyl-tRNA Synthetases]]. Active as [http://en.wikipedia.org/wiki/Serine--tRNA_ligase Serine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.11 6.1.1.11] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SET OCA]. |
==Reference== | ==Reference== | ||
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[[Category: ligase(synthetase)]] | [[Category: ligase(synthetase)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:53:39 2008'' |
Revision as of 14:53, 15 February 2008
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CRYSTAL STRUCTURES AT 2.5 ANGSTROMS RESOLUTION OF SERYL-TRNA SYNTHETASE COMPLEXED WITH TWO DIFFERENT ANALOGUES OF SERYL-ADENYLATE
Overview
Crystal structures of seryl-tRNA synthetase from Thermus thermophilus, complexed with two different analogs of seryl adenylate have been, determined at 2.5 A resolution. The first complex is between the enzyme, and seryl-hydroxamate-AMP (adenosine monophosphate), produced, enzymatically in the crystal from adenosine triphosphate (ATP) and serine, hydroxamate, and the second is with a synthetic analog of seryl adenylate, (5'-O-[N-(L-seryl)-sulfamoyl]adenosine), which is a strong inhibitor of, the enzyme. Both molecules are bound in a similar fashion by a network of, hydrogen bond interactions in a deep hydrophilic cleft formed by the, antiparallel beta sheet and surrounding loops of the synthetase catalytic, domain. Four regions in the primary sequence are involved in the, interactions, including the motif 2 and 3 regions of class 2 synthetases., Apart from the specific recognition of the serine side chain, the, interactions are likely to be similar in all class 2 synthetases.
About this Structure
1SET is a Single protein structure of sequence from Thermus thermophilus with as ligand. The following page contains interesting information on the relation of 1SET with [Aminoacyl-tRNA Synthetases]. Active as Serine--tRNA ligase, with EC number 6.1.1.11 Full crystallographic information is available from OCA.
Reference
Crystal structures at 2.5 angstrom resolution of seryl-tRNA synthetase complexed with two analogs of seryl adenylate., Belrhali H, Yaremchuk A, Tukalo M, Larsen K, Berthet-Colominas C, Leberman R, Beijer B, Sproat B, Als-Nielsen J, Grubel G, et al., Science. 1994 Mar 11;263(5152):1432-6. PMID:8128224
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