1p0b: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
[[Image:1p0b.jpg|left|200px]]
{{Seed}}
[[Image:1p0b.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1p0b|  PDB=1p0b  |  SCENE=  }}  
{{STRUCTURE_1p0b|  PDB=1p0b  |  SCENE=  }}  


'''Crystal Structure Of tRNA-Guanine Transglycosylase (TGT) From Zymomonas mobilis Complexed With Archaeosine Precursor, Preq0'''
===Crystal Structure Of tRNA-Guanine Transglycosylase (TGT) From Zymomonas mobilis Complexed With Archaeosine Precursor, Preq0===




==Overview==
<!--  
The enzyme tRNA-guanine transglycosylase (TGT, EC 2.4.2.29) catalyses a base-exchange reaction that leads to anticodon modifications of certain tRNAs. The TGT enzymes of the eubacteria Zymomonas mobilis (Z. mobilis TGT) and Escherichia coli (E. coli TGT) show a different behaviour in the presence of competitive inhibitors. The active sites of both enzymes are identical apart from a single conservative amino acid exchange, namely Tyr106 of Z. mobilis TGT is replaced by a Phe in E. coli TGT. Although Tyr106 is, in contrast to Phe106, hydrogen bonded in the ligand-free structure, we can show by a mutational study of TGT(Y106F) that this is not the reason for the different responses upon competition. The TGT enzymes of various species differ in their substrate selectivity. Depending on the applied pH conditions and/or induced by ligand binding, a peptide-bond flip modulates the recognition properties of the substrate binding site, which changes between donor and acceptor functionality. Furthermore interstitial water molecules play an important role in these adaptations of the pocket. The flip of the peptide bond is further stabilised by a glutamate residue that operates as general acid/base. An active-site aspartate residue, presumed to operate as a nucleophile through covalent bonding during the base-exchange reaction, shows different conformations depending on the nature of the bound ligand. The induced-fit adaptations observed in the various TGT complex structures by multiple crystal-structure analyses are in agreement with the functional properties of the enzyme. In consequence, full understanding of this plasticity can be exploited for drug design.
The line below this paragraph, {{ABSTRACT_PUBMED_14523925}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 14523925 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_14523925}}


==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Stubbs, M T.]]
[[Category: Stubbs, M T.]]
[[Category: Substrate-protein-complex]]
[[Category: Substrate-protein-complex]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:31:01 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:13:28 2008''

Revision as of 17:13, 28 July 2008

File:1p0b.png

Template:STRUCTURE 1p0b

Crystal Structure Of tRNA-Guanine Transglycosylase (TGT) From Zymomonas mobilis Complexed With Archaeosine Precursor, Preq0

Template:ABSTRACT PUBMED 14523925

About this Structure

1P0B is a Single protein structure of sequence from Zymomonas mobilis. Full crystallographic information is available from OCA.

Reference

Flexible adaptations in the structure of the tRNA-modifying enzyme tRNA-guanine transglycosylase and their implications for substrate selectivity, reaction mechanism and structure-based drug design., Brenk R, Stubbs MT, Heine A, Reuter K, Klebe G, Chembiochem. 2003 Oct 6;4(10):1066-77. PMID:14523925

Page seeded by OCA on Mon Jul 28 20:13:28 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1p0b&oldid=713684"