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| - | [[Image:1rgc.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1rgc| PDB=1rgc | SCENE= }} | | {{STRUCTURE_1rgc| PDB=1rgc | SCENE= }} |
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| - | '''THE COMPLEX BETWEEN RIBONUCLEASE T1 AND 3'-GUANYLIC ACID SUGGESTS GEOMETRY OF ENZYMATIC REACTION PATH. AN X-RAY STUDY'''
| + | ===THE COMPLEX BETWEEN RIBONUCLEASE T1 AND 3'-GUANYLIC ACID SUGGESTS GEOMETRY OF ENZYMATIC REACTION PATH. AN X-RAY STUDY=== |
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| - | ==Overview==
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| - | The crystal structure of the complex between ribonuclease T1 and 3'GMP suggests that (a) a substrate GpN is bound to the active site of ribonuclease T1 in a conformation that actively supports the catalytic process, (b) the reaction occurs in an in-line process, (c) His40 N epsilon H+ activates O2'-H, (d) Glu58 carboxylate acts as base and His92 N epsilon H+ as acid in a general acid-base catalysis. The crystals have the monoclinic space group P2(1), a = 4.968 nm, b = 4.833 nm, c = 4.048 nm, beta = 90.62 degrees with two molecules in the asymmetric unit. The structure was determined by molecular replacement and refined to R = 15.3% with 11,338 data > or = 1 sigma (Fo) in the resolution range 1.0-0.2 nm; this includes 180 water molecules and two Ca2+. The structure of ribonuclease T1 is as previously observed. 3'GMP is bound in syn conformation; guanine is located in the specific recognition site, the ribose adopts C4'-exo puckering, the ribose phosphate is extended with torsion angle epsilon in trans. The O2'-H group is activated by accepting and donating hydrogen bonds from His40 N epsilon H+ and to Glu58 O epsilon 1; the phosphate is hydrogen bonded to Glu58 O epsilon 2H, Arg77 N epsilon H+ and N eta 2H+, Tyr38 O eta H, His92 N eta H+. The conformation of ribose phosphate is such that O2' is at a distance of 0.31 nm from phosphorus, and opposite the P-OP3 bond which accepts a hydrogen bond from His92 N epsilon H+; we infer from a model building study that this bond is equivalent to the scissile P-O5' in a substrate GpN. | + | The line below this paragraph, {{ABSTRACT_PUBMED_8281918}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8281918 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8281918}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Saenger, W.]] | | [[Category: Saenger, W.]] |
| | [[Category: Schindelin, H.]] | | [[Category: Schindelin, H.]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:27:48 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:57:53 2008'' |
Revision as of 20:57, 28 July 2008
Template:STRUCTURE 1rgc
THE COMPLEX BETWEEN RIBONUCLEASE T1 AND 3'-GUANYLIC ACID SUGGESTS GEOMETRY OF ENZYMATIC REACTION PATH. AN X-RAY STUDY
Template:ABSTRACT PUBMED 8281918
About this Structure
1RGC is a Single protein structure of sequence from Aspergillus oryzae. Full crystallographic information is available from OCA.
Reference
The complex between ribonuclease T1 and 3'GMP suggests geometry of enzymic reaction path. An X-ray study., Heydenreich A, Koellner G, Choe HW, Cordes F, Kisker C, Schindelin H, Adamiak R, Hahn U, Saenger W, Eur J Biochem. 1993 Dec 15;218(3):1005-12. PMID:8281918
Page seeded by OCA on Mon Jul 28 23:57:53 2008
