1ys1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (00:42, 21 November 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1ys1.gif|left|200px]]
 
-
{{Structure
+
==Burkholderia cepacia lipase complexed with hexylphosphonic acid (R)-2-methyl-3-phenylpropyl ester==
-
|PDB= 1ys1 |SIZE=350|CAPTION= <scene name='initialview01'>1ys1</scene>, resolution 1.10&Aring;
+
<StructureSection load='1ys1' size='340' side='right'caption='[[1ys1]], [[Resolution|resolution]] 1.10&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=2HR:HEXYLPHOSPHONIC+ACID+(R)-2-METHYL-3-PHENYLPROPYL+ESTER'>2HR</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
+
<table><tr><td colspan='2'>[[1ys1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_cepacia Burkholderia cepacia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YS1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YS1 FirstGlance]. <br>
-
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </span>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.1&#8491;</td></tr>
-
|GENE=
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2HR:HEXYLPHOSPHONIC+ACID+(R)-2-METHYL-3-PHENYLPROPYL+ESTER'>2HR</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-
|DOMAIN=
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ys1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ys1 OCA], [https://pdbe.org/1ys1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ys1 RCSB], [https://www.ebi.ac.uk/pdbsum/1ys1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ys1 ProSAT]</span></td></tr>
-
|RELATEDENTRY=[[3lip|3LIP]]
+
</table>
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ys1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ys1 OCA], [http://www.ebi.ac.uk/pdbsum/1ys1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ys1 RCSB]</span>
+
== Function ==
-
}}
+
[https://www.uniprot.org/uniprot/LIP_BURCE LIP_BURCE] Catalyzes the hydrolysis of triglycerides.
 +
== 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/ys/1ys1_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1ys1 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Synthetic chemists often exploit the high enantioselectivity of lipases to prepare pure enantiomers of primary alcohols, but the molecular basis for this enantioselectivity is unknown. The crystal structures of two phosphonate transition-state analogs bound to Burkholderia cepacia lipase reveal this molecular basis for a typical primary alcohol: 2-methyl-3-phenyl-1-propanol. The enantiomeric alcohol moieties adopt surprisingly similar orientations, with only subtle differences that make it difficult to predict how to alter enantioselectivity. These structures, along with a survey of previous structures of enzyme bound enantiomers, reveal that binding of enantiomers does not involve an exchange of two substituent positions as most researchers assumed. Instead, the enantiomers adopt mirror-image packing, where three of the four substituents at the stereocenter lie in similar positions. The fourth substituent, hydrogen, points in opposite directions.
-
'''Burkholderia cepacia lipase complexed with hexylphosphonic acid (R)-2-methyl-3-phenylpropyl ester'''
+
Mirror-image packing in enantiomer discrimination molecular basis for the enantioselectivity of B.cepacia lipase toward 2-methyl-3-phenyl-1-propanol.,Mezzetti A, Schrag JD, Cheong CS, Kazlauskas RJ Chem Biol. 2005 Apr;12(4):427-37. PMID:15850979<ref>PMID:15850979</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1ys1" style="background-color:#fffaf0;"></div>
-
==Overview==
+
==See Also==
-
Synthetic chemists often exploit the high enantioselectivity of lipases to prepare pure enantiomers of primary alcohols, but the molecular basis for this enantioselectivity is unknown. The crystal structures of two phosphonate transition-state analogs bound to Burkholderia cepacia lipase reveal this molecular basis for a typical primary alcohol: 2-methyl-3-phenyl-1-propanol. The enantiomeric alcohol moieties adopt surprisingly similar orientations, with only subtle differences that make it difficult to predict how to alter enantioselectivity. These structures, along with a survey of previous structures of enzyme bound enantiomers, reveal that binding of enantiomers does not involve an exchange of two substituent positions as most researchers assumed. Instead, the enantiomers adopt mirror-image packing, where three of the four substituents at the stereocenter lie in similar positions. The fourth substituent, hydrogen, points in opposite directions.
+
*[[Lipase 3D Structures|Lipase 3D Structures]]
-
 
+
== References ==
-
==About this Structure==
+
<references/>
-
1YS1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Burkholderia_cepacia Burkholderia cepacia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YS1 OCA].
+
__TOC__
-
 
+
</StructureSection>
-
==Reference==
+
-
Mirror-image packing in enantiomer discrimination molecular basis for the enantioselectivity of B.cepacia lipase toward 2-methyl-3-phenyl-1-propanol., Mezzetti A, Schrag JD, Cheong CS, Kazlauskas RJ, Chem Biol. 2005 Apr;12(4):427-37. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15850979 15850979]
+
[[Category: Burkholderia cepacia]]
[[Category: Burkholderia cepacia]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Triacylglycerol lipase]]
+
[[Category: Cheong CS]]
-
[[Category: Cheong, C S.]]
+
[[Category: Kazlauskas RJ]]
-
[[Category: Kazlauskas, R J.]]
+
[[Category: Mezzetti A]]
-
[[Category: Mezzetti, A.]]
+
[[Category: Schrag JD]]
-
[[Category: Schrag, J D.]]
+
-
[[Category: ca2+ ion]]
+
-
[[Category: cis peptide leu 234]]
+
-
[[Category: inhibitor hexylphosphonic acid (r) 2-methyl-3-phenylpropyl ester]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:20:08 2008''
+

Current revision

Burkholderia cepacia lipase complexed with hexylphosphonic acid (R)-2-methyl-3-phenylpropyl ester

PDB ID 1ys1

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ys1"
Personal tools