3enl
From Proteopedia
(New page: 200px<br /><applet load="3enl" size="450" color="white" frame="true" align="right" spinBox="true" caption="3enl, resolution 2.25Å" /> '''REFINED STRUCTURE OF...) |
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| - | [[Image:3enl.jpg|left|200px]]<br /><applet load="3enl" size=" | + | [[Image:3enl.jpg|left|200px]]<br /><applet load="3enl" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="3enl, resolution 2.25Å" /> | caption="3enl, resolution 2.25Å" /> | ||
'''REFINED STRUCTURE OF YEAST APO-ENOLASE AT 2.25 ANGSTROMS RESOLUTION'''<br /> | '''REFINED STRUCTURE OF YEAST APO-ENOLASE AT 2.25 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of apo-enolase from baker's yeast (Saccharomyces | + | The crystal structure of apo-enolase from baker's yeast (Saccharomyces cerevisiae) was established at 2.25 A resolution using a restrained least-squares refinement method. Based on 21,077 independent reflections of better than 8 A resolution, a final R-factor of 15.4% was obtained with a model obeying standard geometry within 0.017 A in bond length and 3.5 degrees in bond angles. The upper limit for the co-ordinate accuracy of the atoms was estimated to be 0.18 A. The refinement confirmed the heterodox, non-parallel character of the 8-fold beta alpha-barrel domain with beta beta alpha alpha(beta alpha)6 topology. The reported structure for which the data were collected at pH 5.0 represents an apo-form of the enzyme. Of the three carboxylic ligands that form the conformational metal ion binding site two, Glu295 and Asp320, are very close and presumably form a strong acidic type hydrogen bond with the proton partially replacing the electric charge of the physiological cofactor Mg2+. The single sulfate ion found in the structure is in the active site cavity, co-ordinated to the side-chains of Lys345 and Arg374, and to the N atom of Ser375. It is located about 7.4 A from the conformational metal ion binding site. It occupies the site in which the phosphate group of the substrate binds. |
==About this Structure== | ==About this Structure== | ||
| - | 3ENL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. This structure | + | 3ENL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entries 2ENL and 1ENL. Active as [http://en.wikipedia.org/wiki/Phosphopyruvate_hydratase Phosphopyruvate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.11 4.2.1.11] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ENL OCA]. |
==Reference== | ==Reference== | ||
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[[Category: carbon-oxygen lyase]] | [[Category: carbon-oxygen lyase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:09:10 2008'' |
Revision as of 17:09, 21 February 2008
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REFINED STRUCTURE OF YEAST APO-ENOLASE AT 2.25 ANGSTROMS RESOLUTION
Overview
The crystal structure of apo-enolase from baker's yeast (Saccharomyces cerevisiae) was established at 2.25 A resolution using a restrained least-squares refinement method. Based on 21,077 independent reflections of better than 8 A resolution, a final R-factor of 15.4% was obtained with a model obeying standard geometry within 0.017 A in bond length and 3.5 degrees in bond angles. The upper limit for the co-ordinate accuracy of the atoms was estimated to be 0.18 A. The refinement confirmed the heterodox, non-parallel character of the 8-fold beta alpha-barrel domain with beta beta alpha alpha(beta alpha)6 topology. The reported structure for which the data were collected at pH 5.0 represents an apo-form of the enzyme. Of the three carboxylic ligands that form the conformational metal ion binding site two, Glu295 and Asp320, are very close and presumably form a strong acidic type hydrogen bond with the proton partially replacing the electric charge of the physiological cofactor Mg2+. The single sulfate ion found in the structure is in the active site cavity, co-ordinated to the side-chains of Lys345 and Arg374, and to the N atom of Ser375. It is located about 7.4 A from the conformational metal ion binding site. It occupies the site in which the phosphate group of the substrate binds.
About this Structure
3ENL is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. This structure supersedes the now removed PDB entries 2ENL and 1ENL. Active as Phosphopyruvate hydratase, with EC number 4.2.1.11 Full crystallographic information is available from OCA.
Reference
Refined structure of yeast apo-enolase at 2.25 A resolution., Stec B, Lebioda L, J Mol Biol. 1990 Jan 5;211(1):235-48. PMID:2405163
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