1gsp: Difference between revisions
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|PDB= 1gsp |SIZE=350|CAPTION= <scene name='initialview01'>1gsp</scene>, resolution 2.20Å | |PDB= 1gsp |SIZE=350|CAPTION= <scene name='initialview01'>1gsp</scene>, resolution 2.20Å | ||
|SITE= <scene name='pdbsite=BI1:Site'>BI1</scene>, <scene name='pdbsite=CAL:Site'>CAL</scene> and <scene name='pdbsite=CAT:Active+Site'>CAT</scene> | |SITE= <scene name='pdbsite=BI1:Site'>BI1</scene>, <scene name='pdbsite=CAL:Site'>CAL</scene> and <scene name='pdbsite=CAT:Active+Site'>CAT</scene> | ||
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=SGP:GUANOSINE-2 | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=SGP:GUANOSINE-2',3'-CYCLOPHOSPHOROTHIOATE'>SGP</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Ribonuclease_T(1) Ribonuclease T(1)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.3 3.1.27.3] | |ACTIVITY= [http://en.wikipedia.org/wiki/Ribonuclease_T(1) Ribonuclease T(1)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.3 3.1.27.3] | ||
|GENE= | |GENE= | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 11:59:01 2008'' | ||
Revision as of 12:59, 23 March 2008
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| , resolution 2.20Å | |||||||
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| Sites: | , and | ||||||
| Ligands: | and | ||||||
| Activity: | Ribonuclease T(1), with EC number 3.1.27.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
RIBONUCLEASE T1 COMPLEXED WITH 2',3'-CGPS, 1 DAY
OverviewOverview
Here we present a time-resolved crystallographic analysis of the hydrolysis of exo (Sp) guanosine 2',3'-cyclophosphorothioate by RNase T1. The use of a slow substrate and fast crystallization methods made it possible to perform the study with conventional data-collection techniques. The results support the idea that the hydrolysis reaction proceeds through a mechanism that is the inverse of the transesterification reaction. In addition, the structures provide an explanation for the differential behavior of RNase T1 towards exo- and endo-cyclic thiophosphates.
About this StructureAbout this Structure
1GSP is a Single protein structure of sequence from Aspergillus oryzae. Full crystallographic information is available from OCA.
ReferenceReference
Hydrolysis of a slow cyclic thiophosphate substrate of RNase T1 analyzed by time-resolved crystallography., Zegers I, Loris R, Dehollander G, Fattah Haikal A, Poortmans F, Steyaert J, Wyns L, Nat Struct Biol. 1998 Apr;5(4):280-3. PMID:9546218
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