2aat
From Proteopedia
(New page: 200px<br /><applet load="2aat" size="450" color="white" frame="true" align="right" spinBox="true" caption="2aat, resolution 2.8Å" /> '''2.8-ANGSTROMS-RESOLUT...) |
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| - | [[Image:2aat.jpg|left|200px]]<br /><applet load="2aat" size=" | + | [[Image:2aat.jpg|left|200px]]<br /><applet load="2aat" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2aat, resolution 2.8Å" /> | caption="2aat, resolution 2.8Å" /> | ||
'''2.8-ANGSTROMS-RESOLUTION CRYSTAL STRUCTURE OF AN ACTIVE-SITE MUTANT OF ASPARTATE AMINOTRANSFERASE FROM ESCHERICHIA COLI'''<br /> | '''2.8-ANGSTROMS-RESOLUTION CRYSTAL STRUCTURE OF AN ACTIVE-SITE MUTANT OF ASPARTATE AMINOTRANSFERASE FROM ESCHERICHIA COLI'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of a mutant of the aspartate | + | The three-dimensional structure of a mutant of the aspartate aminotransferase from Escherichia coli, in which the active-site lysine has been substituted by alanine (K258A), has been determined at 2.8-A resolution by X-ray diffraction. The mutant enzyme contains pyridoxamine phosphate as cofactor. The structure is compared to that of the mitochondrial aspartate aminotransferase. The most striking differences, aside from the absence of the lysine side chain, occur in the positions of the pyridoxamine group and of tryptophan 140. |
==About this Structure== | ==About this Structure== | ||
| - | 2AAT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 and PMP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] Full crystallographic information is available from [http:// | + | 2AAT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=PMP:'>PMP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AAT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transferase(aminotransferase)]] | [[Category: transferase(aminotransferase)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:25:39 2008'' |
Revision as of 14:25, 21 February 2008
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2.8-ANGSTROMS-RESOLUTION CRYSTAL STRUCTURE OF AN ACTIVE-SITE MUTANT OF ASPARTATE AMINOTRANSFERASE FROM ESCHERICHIA COLI
Overview
The three-dimensional structure of a mutant of the aspartate aminotransferase from Escherichia coli, in which the active-site lysine has been substituted by alanine (K258A), has been determined at 2.8-A resolution by X-ray diffraction. The mutant enzyme contains pyridoxamine phosphate as cofactor. The structure is compared to that of the mitochondrial aspartate aminotransferase. The most striking differences, aside from the absence of the lysine side chain, occur in the positions of the pyridoxamine group and of tryptophan 140.
About this Structure
2AAT is a Single protein structure of sequence from Escherichia coli with and as ligands. Active as Aspartate transaminase, with EC number 2.6.1.1 Full crystallographic information is available from OCA.
Reference
2.8-A-resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coli., Smith DL, Almo SC, Toney MD, Ringe D, Biochemistry. 1989 Oct 3;28(20):8161-7. PMID:2513875
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