This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

4leq

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 12:18, 11 August 2016

tRNA guanine transglycosylase (TGT) in complex with Furanoside-Based lin-Benzoguanine 1

Structural highlights

4leq is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Related:	4lbu, 4kwo, 2z7k, 3eos, 1pud
Activity:	tRNA-guanine(34) transglycosylase, with EC number 2.4.2.29
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TGT_ZYMMO] Exchanges the guanine residue with 7-aminomethyl-7-deazaguanine in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). After this exchange, a cyclopentendiol moiety is attached to the 7-aminomethyl group of 7-deazaguanine, resulting in the hypermodified nucleoside queuosine (Q) (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).[HAMAP-Rule:MF_00168]

Publication Abstract from PubMed

The enzyme tRNA-guanine transglycosylase has been identified as a drug target for the foodborne illness shigellosis. A key challenge in structure-based design for this enzyme is the filling of the polar ribose-34 pocket. Herein, we describe a novel series of ligands consisting of furanoside-appended lin-benzoguanines. They were designed to replace a conserved water cluster and differ by the functional groups at C(2) and C(3) of the furanosyl moiety being either OH or OMe. The unfavorable desolvation of Asp102 and Asp280, which are located close to the ribose-34 pocket, had a significant impact on binding affinity. While the enzyme has tRNA as its natural substrate, X-ray co-crystal structures revealed that the furanosyl moieties of the ligands are not accommodated in the tRNA ribose-34 site, but at the location of the adjacent phosphate group. A remarkable similarity of the position of the oxygen atoms in these two structures suggests furanosides as a potential phosphate isoster.

Replacement of Water Molecules in a Phosphate Binding Site by Furanoside-Appended lin-Benzoguanine Ligands of tRNA-Guanine Transglycosylase (TGT).,Barandun LJ, Ehrmann FR, Zimmerli D, Immekus F, Giroud M, Grunenfelder C, Schweizer WB, Bernet B, Betz M, Heine A, Klebe G, Diederich F Chemistry. 2015 Jan 2;21(1):126-35. doi: 10.1002/chem.201405764. Epub 2014 Dec 5. PMID:25483606^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Barandun LJ, Ehrmann FR, Zimmerli D, Immekus F, Giroud M, Grunenfelder C, Schweizer WB, Bernet B, Betz M, Heine A, Klebe G, Diederich F. Replacement of Water Molecules in a Phosphate Binding Site by Furanoside-Appended lin-Benzoguanine Ligands of tRNA-Guanine Transglycosylase (TGT). Chemistry. 2015 Jan 2;21(1):126-35. doi: 10.1002/chem.201405764. Epub 2014 Dec 5. PMID:25483606 doi:http://dx.doi.org/10.1002/chem.201405764

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4leq"

@@ Line 1: / Line 1: @@
 ==tRNA guanine transglycosylase (TGT) in complex with Furanoside-Based lin-Benzoguanine 1==
 <StructureSection load='4leq' size='340' side='right' caption='[[4leq]], [[Resolution|resolution]] 1.41&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4lbu|4lbu]], [[4kwo|4kwo]], [[2z7k|2z7k]], [[3eos|3eos]], [[1pud|1pud]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/tRNA-guanine(34)_transglycosylase tRNA-guanine(34) transglycosylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.29 2.4.2.29] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4leq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4leq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4leq RCSB], [http://www.ebi.ac.uk/pdbsum/4leq PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4leq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4leq OCA], [http://pdbe.org/4leq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4leq RCSB], [http://www.ebi.ac.uk/pdbsum/4leq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4leq ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4leq" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[TRNA-guanine transglycosylase|TRNA-guanine transglycosylase]]
 == References ==
 <references/>

4leq

From Proteopedia

Revision as of 12:18, 11 August 2016

tRNA guanine transglycosylase (TGT) in complex with Furanoside-Based lin-Benzoguanine 1

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox