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1enu

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Revision as of 14:52, 8 July 2020

A new target for shigellosis: Rational design and crystallographic studies of inhibitors of tRNA-guanine transglycosylase

Structural highlights

1enu is a 1 chain structure with sequence from Zymomonas mobilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1efz, 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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Eubacterial tRNA-guanine transglycosylase (TGT) is involved in the hyper-modification of cognate tRNAs leading to the exchange of G34 at the wobble position in the anticodon loop by preQ1 (2-amino-5-(aminomethyl)pyrrolo[2,3-d]pyrimidin-4(3H)-one) as part of the biosynthesis of queuine (Q). Mutation of the tgt gene in Shigella flexneri results in a significant loss of pathogenicity of the bacterium, revealing TGT as a new target for the design of potent drugs against Shigellosis. The X-ray structure of Zymomonas mobilis TGT in complex with preQ1 was used to search for new putative inhibitors with the computer program LUDI. An initial screen of the Available Chemical Directory, a database compiled from commercially available compounds, suggested several hits. Of these, 4-aminophthalhydrazide (APH) showed an inhibition constant in the low micromolar range. The 1.95 A crystal structure of APH in complex with Z. mobilis TGT served as a starting point for further modification of this initial lead.

A new target for shigellosis: rational design and crystallographic studies of inhibitors of tRNA-guanine transglycosylase.,Gradler U, Gerber HD, Goodenough-Lashua DM, Garcia GA, Ficner R, Reuter K, Stubbs MT, Klebe G J Mol Biol. 2001 Feb 23;306(3):455-67. PMID:11178905^[1]

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

References

↑ Gradler U, Gerber HD, Goodenough-Lashua DM, Garcia GA, Ficner R, Reuter K, Stubbs MT, Klebe G. A new target for shigellosis: rational design and crystallographic studies of inhibitors of tRNA-guanine transglycosylase. J Mol Biol. 2001 Feb 23;306(3):455-67. PMID:11178905 doi:10.1006/jmbi.2000.4256

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1enu"

@@ Line 1: / Line 1: @@
 ==A new target for shigellosis: Rational design and crystallographic studies of inhibitors of tRNA-guanine transglycosylase==
-<StructureSection load='1enu' size='340' side='right' caption='[[1enu]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
+<StructureSection load='1enu' size='340' side='right'caption='[[1enu]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1enu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Zymomonas_mobilis Zymomonas mobilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ENU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ENU FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1enu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Zymomonas_mobilis Zymomonas mobilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ENU OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1ENU FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=APZ:4-AMINOPHTHALHYDRAZIDE'>APZ</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=APZ:4-AMINOPHTHALHYDRAZIDE'>APZ</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1efz|1efz]], [[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=1enu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1enu OCA], [http://pdbe.org/1enu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1enu RCSB], [http://www.ebi.ac.uk/pdbsum/1enu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1enu ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1enu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1enu OCA], [http://pdbe.org/1enu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1enu RCSB], [http://www.ebi.ac.uk/pdbsum/1enu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1enu ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 37: / Line 37: @@
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Zymomonas mobilis]]
 [[Category: Ficner, R]]

1enu

From Proteopedia

Revision as of 14:52, 8 July 2020

A new target for shigellosis: Rational design and crystallographic studies of inhibitors of tRNA-guanine transglycosylase

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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