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.

1nvk

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

T4 phage BGT in complex with UDP and a Mn2+ ion at 1.8 A resolution

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
-[[Image:1nvk.jpg|left|200px]]<br /><applet load="1nvk" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1nvk, resolution 1.8&Aring;" />
-'''T4 phage BGT in complex with UDP and a Mn2+ ion at 1.8 A resolution'''<br />
-==Overview==
+==T4 phage BGT in complex with UDP and a Mn2+ ion at 1.8 A resolution==
-T4 phage beta-glucosyltransferase (BGT) is an inverting, glycosyltransferase (GT) that transfers glucose from uridine, diphospho-glucose (UDP-glucose) to an acceptor modified DNA. BGT belongs, to the GT-B structural superfamily, represented, so far, by five different, inverting or retaining GT families. Here, we report three high-resolution, X-ray structures of BGT and a point mutant solved in the presence of, UDP-glucose. The two co-crystal structures of the D100A mutant show that, unlike the wild-type enzyme, this mutation prevents glucose hydrolysis., This strongly indicates that Asp100 is the catalytic base. We obtained the, wild-type BGT-UDP-glucose complex by soaking substrate-free BGT crystals., Comparison with a previous structure of BGT solved in the presence of the, donor product UDP and an acceptor analogue provides the first model of an, inverting GT-B enzyme in which both the donor and acceptor substrates are, bound to the active site. The structural analyses support the in-line, displacement reaction mechanism previously proposed, locate residues, involved in donor substrate specificity and identify the catalytic base.
+<StructureSection load='1nvk' size='340' side='right'caption='[[1nvk]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+== Structural highlights ==
-==About this Structure==
+<table><tr><td colspan='2'>[[1nvk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NVK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NVK FirstGlance]. <br>
-NVK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] with MN, UDP and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/DNA_beta-glucosyltransferase DNA beta-glucosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.27 2.4.1.27] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NVK OCA].
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>
-==Reference==
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nvk OCA], [https://pdbe.org/1nvk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nvk RCSB], [https://www.ebi.ac.uk/pdbsum/1nvk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nvk ProSAT]</span></td></tr>
-Crystal structures of the T4 phage beta-glucosyltransferase and the D100A mutant in complex with UDP-glucose: glucose binding and identification of the catalytic base for a direct displacement mechanism., Lariviere L, Gueguen-Chaignon V, Morera S, J Mol Biol. 2003 Jul 25;330(5):1077-86. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12860129 12860129]
+</table>
-[[Category: Bacteriophage t4]]
+== Function ==
-[[Category: DNA beta-glucosyltransferase]]
+[https://www.uniprot.org/uniprot/GSTB_BPT4 GSTB_BPT4] Catalyzes the transfer of glucose (Glc) from uridine diphosphoglucose (UDP-Glc) to 5-hydroxymethylcytosine (5-HMC) in double-stranded DNA. Is involved in a DNA modification process to protect the phage genome against its own nucleases and the host restriction endonuclease system.
-[[Category: Single protein]]
+__TOC__
-[[Category: Gueguen-Chaignon, V.]]
+</StructureSection>
-[[Category: Kurzeck, J.]]
+[[Category: Escherichia virus T4]]
-[[Category: Lariviere, L.]]
+[[Category: Large Structures]]
-[[Category: Morera, S.]]
+[[Category: Gueguen-Chaignon V]]
-[[Category: Rueger, W.]]
+[[Category: Kurzeck J]]
-[[Category: GOL]]
+[[Category: Lariviere L]]
-[[Category: MN]]
+[[Category: Morera S]]
-[[Category: UDP]]
+[[Category: Rueger W]]
-[[Category: glycosyltransferase]]
-[[Category: gt-b]]
-[[Category: mn]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:35:31 2007''

1nvk

From Proteopedia

Current revision

T4 phage BGT in complex with UDP and a Mn2+ ion at 1.8 A resolution

Structural highlights

Function

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox