1rgc
From Proteopedia
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[[Image:1rgc.gif|left|200px]] | [[Image:1rgc.gif|left|200px]] | ||
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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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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:[http://www.ncbi.nlm.nih.gov/pubmed/8281918 8281918] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8281918 8281918] | ||
[[Category: Aspergillus oryzae]] | [[Category: Aspergillus oryzae]] | ||
| - | [[Category: Ribonuclease T(1)]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Adamiak, R.]] | [[Category: Adamiak, R.]] | ||
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[[Category: Saenger, W.]] | [[Category: Saenger, W.]] | ||
[[Category: Schindelin, H.]] | [[Category: Schindelin, H.]] | ||
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Revision as of 04:27, 3 May 2008
THE COMPLEX BETWEEN RIBONUCLEASE T1 AND 3'-GUANYLIC ACID SUGGESTS GEOMETRY OF ENZYMATIC REACTION PATH. AN X-RAY STUDY
Overview
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.
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 Sat May 3 07:27:48 2008
