1v1d

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (13:24, 9 May 2024) (edit) (undo)
 
(13 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1v1d.gif|left|200px]]
 
-
{{Structure
+
==Nucleophilic and General Acid Catalysis at Physiological pH by a Designed Miniature Esterase==
-
|PDB= 1v1d |SIZE=350|CAPTION= <scene name='initialview01'>1v1d</scene>
+
<StructureSection load='1v1d' size='340' side='right'caption='[[1v1d]]' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND=
+
<table><tr><td colspan='2'>[[1v1d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1V1D FirstGlance]. <br>
-
|ACTIVITY=
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-
|GENE=
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1v1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v1d OCA], [https://pdbe.org/1v1d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v1d RCSB], [https://www.ebi.ac.uk/pdbsum/1v1d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v1d ProSAT]</span></td></tr>
-
}}
+
</table>
-
 
+
== Function ==
-
'''NUCLEOPHILIC AND GENERAL ACID CATALYSIS AT PHYSIOLOGICAL PH BY A DESIGNED MINIATURE ESTERASE'''
+
[https://www.uniprot.org/uniprot/PAHO_BOVIN PAHO_BOVIN] Pancreatic hormone is synthesized in pancreatic islets of Langerhans and acts as a regulator of pancreatic and gastrointestinal functions.
-
 
+
== Evolutionary Conservation ==
-
 
+
[[Image:Consurf_key_small.gif|200px|right]]
-
==Overview==
+
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/main_output.php?pdb_ID=1v1d 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.
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.
-
==About this Structure==
+
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>
-
1V1D is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V1D OCA].
+
-
 
+
-
==Reference==
+
-
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:[http://www.ncbi.nlm.nih.gov/pubmed/15280952 15280952]
+
-
[[Category: Single protein]]
+
-
[[Category: Allemann, R K.]]
+
-
[[Category: Nicoll, A.]]
+
-
[[Category: cleavage on pair of basic residue]]
+
-
[[Category: hormone]]
+
-
[[Category: pancrea]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:39:37 2008''
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1v1d" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Bos taurus]]
 +
[[Category: Large Structures]]
 +
[[Category: Allemann RK]]
 +
[[Category: Nicoll A]]

Current revision

Nucleophilic and General Acid Catalysis at Physiological pH by a Designed Miniature Esterase

PDB ID 1v1d

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"
Personal tools