1v1d

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "1v1d" [edit=sysop:move=sysop])
Line 1: Line 1:
-
[[Image:1v1d.png|left|200px]]
+
==NUCLEOPHILIC AND GENERAL ACID CATALYSIS AT PHYSIOLOGICAL PH BY A DESIGNED MINIATURE ESTERASE==
 +
<StructureSection load='1v1d' size='340' side='right' caption='[[1v1d]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1v1d]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V1D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1V1D FirstGlance]. <br>
 +
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bba|1bba]], [[1ljv|1ljv]]</td></tr>
 +
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v1d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1v1d RCSB], [http://www.ebi.ac.uk/pdbsum/1v1d PDBsum]</span></td></tr>
 +
<table>
 +
== 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/v1/1v1d_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/chain_selection.php?pdb_ID=2ata ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
A 31-residue peptide (Art-Est) was designed to catalyse the hydrolysis of p-nitrophenyl esters through histidine catalysis on the solvent exposed face of the alpha-helix of bovine pancreatic polypeptide. NMR spectroscopy indicated that Art-Est adopted a stable 3-dimensional structure in solution. Art-Est was an efficient catalyst with second order rate constants of up to 0.050 M(-1) s(-1). The activity of Art-Est was a consequence of the increased nucleophilicity of His-22, which had a reduced pK(a) value of 5.5 as a consequence of its interaction with His-18 and the positively charged Arg-25 and Arg-26. Mass spectrometry and NMR spectroscopy confirmed that the Art-Est catalysed hydrolysis of p-nitrophenyl esters proceeded through an acyl-enzyme intermediate. A solvent kinetic isotope effect of 1.8 indicated that the transition state preceding the acyl intermediate was stabilised through interaction with the protonated side-chain of His-18 and indicated a reaction mechanism similar to that generally observed for natural esterases. The involvement in the reaction of two histidine residues with different pK(a) values led to a bell-shaped dependence of the reaction rate on the pH of the solution. The catalytic behaviour of Art-Est indicated that designed miniature enzymes can act in a transparent mechanism based fashion with enzyme-like behaviour through the interplay of several amino acid residues.
-
{{STRUCTURE_1v1d| PDB=1v1d | SCENE= }}
+
Nucleophilic and general acid catalysis at physiological pH by a designed miniature esterase.,Nicoll AJ, Allemann RK Org Biomol Chem. 2004 Aug 7;2(15):2175-80. Epub 2004 Jul 8. PMID:15280952<ref>PMID:15280952</ref>
-
===NUCLEOPHILIC AND GENERAL ACID CATALYSIS AT PHYSIOLOGICAL PH BY A DESIGNED MINIATURE ESTERASE===
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
{{ABSTRACT_PUBMED_15280952}}
+
== References ==
-
 
+
<references/>
-
==About this Structure==
+
__TOC__
-
[[1v1d]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V1D OCA].
+
</StructureSection>
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:015280952</ref><references group="xtra"/>
+
[[Category: Allemann, R K.]]
[[Category: Allemann, R K.]]
[[Category: Nicoll, A.]]
[[Category: Nicoll, A.]]

Revision as of 21:56, 29 September 2014

NUCLEOPHILIC AND GENERAL ACID CATALYSIS AT PHYSIOLOGICAL PH BY A DESIGNED MINIATURE ESTERASE

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://proteopedia.org/wiki/index.php/1v1d"
Views
Personal tools
Navigation
Toolbox