1syl

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:27, 25 October 2023) (edit) (undo)
 
(13 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:1syl.png|left|200px]]
 
-
<!--
+
==Crystal structure of inactive mutant dUTPase complexed with substrate dUTP==
-
The line below this paragraph, containing "STRUCTURE_1syl", creates the "Structure Box" on the page.
+
<StructureSection load='1syl' size='340' side='right'caption='[[1syl]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[1syl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SYL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SYL FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DUT:DEOXYURIDINE-5-TRIPHOSPHATE'>DUT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
-
{{STRUCTURE_1syl| PDB=1syl | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1syl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1syl OCA], [https://pdbe.org/1syl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1syl RCSB], [https://www.ebi.ac.uk/pdbsum/1syl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1syl ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/DUT_ECOLI DUT_ECOLI] This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.[HAMAP-Rule:MF_00116]
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sy/1syl_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1syl ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
dUTPase is essential to keep uracil out of DNA. Crystal structures of substrate (dUTP and alpha,beta-imino-dUTP) and product complexes of wild type and mutant dUTPases were determined to reveal how an enzyme responsible for DNA integrity functions. A kinetic analysis of wild type and mutant dUTPases was performed to obtain relevant mechanistic information in solution. Substrate hydrolysis is shown to be initiated via in-line nucleophile attack of a water molecule oriented by an activating conserved aspartate residue. Substrate binding in a catalytically competent conformation is achieved by (i) multiple interactions of the triphosphate moiety with catalysis-assisting Mg2+, (ii) a concerted motion of residues from three conserved enzyme motifs as compared with the apoenzyme, and (iii) an intricate hydrogen-bonding network that includes several water molecules in the active site. Results provide an understanding for the catalytic role of conserved residues in dUTPases.
-
===Crystal structure of inactive mutant dUTPase complexed with substrate dUTP===
+
Structural insights into the catalytic mechanism of phosphate ester hydrolysis by dUTPase.,Barabas O, Pongracz V, Kovari J, Wilmanns M, Vertessy BG J Biol Chem. 2004 Oct 8;279(41):42907-15. Epub 2004 Jun 17. PMID:15208312<ref>PMID:15208312</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1syl" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_15208312}}, adds the Publication Abstract to the page
+
*[[DUTPase 3D structures|DUTPase 3D structures]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 15208312 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_15208312}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
1SYL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SYL OCA].
+
-
 
+
-
==Reference==
+
-
Structural insights into the catalytic mechanism of phosphate ester hydrolysis by dUTPase., Barabas O, Pongracz V, Kovari J, Wilmanns M, Vertessy BG, J Biol Chem. 2004 Oct 8;279(41):42907-15. Epub 2004 Jun 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15208312 15208312]
+
-
 
+
-
Atomic resolution structure of Escherichia coli dUTPase determined ab initio., Gonzalez A, Larsson G, Persson R, Cedergren-Zeppezauer E, Acta Crystallogr D Biol Crystallogr. 2001 Jun;57(Pt 6):767-74. Epub 2001, May 25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11375495 11375495]
+
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: DUTP diphosphatase]]
+
[[Category: Barabas O]]
-
[[Category: Barabas, O.]]
+
[[Category: Kovari J]]
-
[[Category: Kovari, J.]]
+
[[Category: Pongracz V]]
-
[[Category: Pongracz, V.]]
+
[[Category: Vertessy BG]]
-
[[Category: Vertessy, B G.]]
+
[[Category: Wilmanns M]]
-
[[Category: Wilmanns, M.]]
+
-
[[Category: Enzyme-ligand complex]]
+
-
[[Category: Jelly roll]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:27:50 2008''
+

Current revision

Crystal structure of inactive mutant dUTPase complexed with substrate dUTP

PDB ID 1syl

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools