3aat

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[[Image:3aat.gif|left|200px]]
[[Image:3aat.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 3aat |SIZE=350|CAPTION= <scene name='initialview01'>3aat</scene>, resolution 2.8&Aring;
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The line below this paragraph, containing "STRUCTURE_3aat", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5&#39;-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_3aat| PDB=3aat | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3aat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aat OCA], [http://www.ebi.ac.uk/pdbsum/3aat PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3aat RCSB]</span>
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}}
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'''ACTIVITY AND STRUCTURE OF THE ACTIVE-SITE MUTANTS R386Y AND R386F OF ESCHERICHIA COLI ASPARTATE AMINOTRANSFERASE'''
'''ACTIVITY AND STRUCTURE OF THE ACTIVE-SITE MUTANTS R386Y AND R386F OF ESCHERICHIA COLI ASPARTATE AMINOTRANSFERASE'''
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[[Category: Petsko, G A.]]
[[Category: Petsko, G A.]]
[[Category: Ringe, D.]]
[[Category: Ringe, D.]]
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[[Category: transferase(aminotransferase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:18:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:22:12 2008''
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Revision as of 17:18, 4 May 2008

Image:3aat.gif

Template:STRUCTURE 3aat

ACTIVITY AND STRUCTURE OF THE ACTIVE-SITE MUTANTS R386Y AND R386F OF ESCHERICHIA COLI ASPARTATE AMINOTRANSFERASE


Overview

Arginine-386, the active-site residue of Escherichia coli aspartate aminotransferase (EC 2.6.1.1) that binds the substrate alpha-carboxylate, was replaced with tyrosine and phenylalanine by site-directed mutagenesis. This experiment was undertaken to elucidate the roles of particular enzyme-substrate interactions in triggering the substrate-induced conformational change in the enzyme. The activity and crystal structure of the resulting mutants were examined. The apparent second-order rate constants of both of these mutants are reduced by more than 5 orders of magnitude as compared to that of wild-type enzyme, though R386Y is slightly more active than R386F. The 2.5-A resolution structure of R386F in its native state was determined by using difference Fourier methods. The overall structure is very similar to that of the wild-type enzyme in the open conformation. The position of the Phe-386 side chain, however, appears to shift with respect to that of Arg-386 in the wild-type enzyme and to form new contacts with neighboring residues.

About this Structure

3AAT is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Activity and structure of the active-site mutants R386Y and R386F of Escherichia coli aspartate aminotransferase., Danishefsky AT, Onnufer JJ, Petsko GA, Ringe D, Biochemistry. 1991 Feb 19;30(7):1980-5. PMID:1993208 Page seeded by OCA on Sun May 4 20:18:55 2008

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