1rds: Difference between revisions

Revision as of 23:50, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1rds.png

Template:STRUCTURE 1rds

CRYSTAL STRUCTURE OF RIBONUCLEASE MS (AS RIBONUCLEASE T1 HOMOLOGUE) COMPLEXED WITH A GUANYLYL-3',5'-CYTIDINE ANALOGUECRYSTAL STRUCTURE OF RIBONUCLEASE MS (AS RIBONUCLEASE T1 HOMOLOGUE) COMPLEXED WITH A GUANYLYL-3',5'-CYTIDINE ANALOGUE

Template:ABSTRACT PUBMED 8218254

About this StructureAbout this Structure

1RDS is a Single protein structure of sequence from Aspergillus phoenicis. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of ribonuclease Ms (as a ribonuclease T1 homologue) complexed with a guanylyl-3',5'-cytidine analogue., Nonaka T, Nakamura KT, Uesugi S, Ikehara M, Irie M, Mitsui Y, Biochemistry. 1993 Nov 9;32(44):11825-37. PMID:8218254

Page seeded by OCA on Mon Jul 28 23:50:32 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1rds.gif|left|200px]]
+{{Seed}}
+[[Image:1rds.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1rds|  PDB=1rds  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF RIBONUCLEASE MS (AS RIBONUCLEASE T1 HOMOLOGUE) COMPLEXED WITH A GUANYLYL-3',5'-CYTIDINE ANALOGUE'''
+===CRYSTAL STRUCTURE OF RIBONUCLEASE MS (AS RIBONUCLEASE T1 HOMOLOGUE) COMPLEXED WITH A GUANYLYL-3',5'-CYTIDINE ANALOGUE===
-==Overview==
+<!--
-A ribonuclease T1 homologue, ribonuclease Ms (RNase Ms) from Aspergillus saitoi, has been crystallized as a complex with a substrate analogue GfpC where the 2'-hydroxyl (2'-OH) group of guanosine in guanylyl-3',5'-cytidine (GpC) is replaced by the 2'-fluorine (2'-F) atom to prevent transesterification. The crystal structure of the complex was solved at 1.8-A resolution to a final R-factor of 0.204. The role of His92 (RNase T1 numbering) as the general acid catalyst was confirmed. Of the two alternative candidates for a general base to abstract a proton from the 2'-OH group, His40 and Glu58 were found close to the 2'-F atom, making the decision between the two groups difficult. We then superposed the active site of the RNase Ms/GfpC complex with that of pancreatic ribonuclease S (RNase S) complexed with a substrate analogue UpcA, a phosphonate analogue of uridylyl-3',5'-adenosine (UpA), and found that His12 and His119 of RNase A almost exactly coincided with Glu58 and His92, respectively, of RNase Ms. Similar superposition with a prokaryotic microbial ribonuclease, RNase St [Nakamura, K. T., Iwahashi, K., Yamamoto, Y., Iitaka, Y., Yoshida, N., &amp; Mitsui, Y. (1982) Nature 299, 564-566], also indicated Glu58 as a general base. Thus the present comparative geometrical studies consistently favor, albeit indirectly, the traditional as well as the most recent notion [Steyaert, J., Hallenga, K., Wyns, L., &amp; Stanssens, P. (1990) Biochemistry 29, 9064-9072] that Glu58, rather than His40, must be the general base catalyst in the intact enzymes of the RNase T1 family.
+The line below this paragraph, {{ABSTRACT_PUBMED_8218254}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8218254 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8218254}}
 ==About this Structure==
@@ Line 25: / Line 29: @@
 [[Category: Nakamura, K T.]]
 [[Category: Nonaka, T.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 07:22:21 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:50:32 2008''