1mli: Difference between revisions

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New page: left|200px<br /><applet load="1mli" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mli, resolution 3.3Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1mli.gif|left|200px]]<br /><applet load="1mli" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1mli.gif|left|200px]]<br /><applet load="1mli" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1mli, resolution 3.3&Aring;" />
caption="1mli, resolution 3.3&Aring;" />
'''CRYSTAL STRUCTURE OF MUCONOLACTONE ISOMERASE AT 3.3 ANGSTROMS RESOLUTION'''<br />
'''CRYSTAL STRUCTURE OF MUCONOLACTONE ISOMERASE AT 3.3 ANGSTROMS RESOLUTION'''<br />


==Overview==
==Overview==
The crystal structure of muconolactone isomerase from Pseudomonas putida, a unique molecule with ten 96 amino acid subunits and 5-fold, and 2-fold, symmetries, has been solved at 3.3 A resolution. The non-crystallographic, symmetries were used to refine the initial single isomorphous replacement, phases and produce an interpretable 10-fold averaged map. The backbone, trace is complete and confirmed by the amino acid sequence fit. Each, subunit is composed of a body with two alpha-helices and an antiparallel, twisted beta-sheet of four strands, and an extended arm. The helices and, the sheet fold to form a two-layered structure with an enclosed, hydrophobic core and a partially formed putative active site pocket. The, C-terminal arm of another subunit related by a local dyad symmetry extends, over the core to complete this pocket. The decameric protein is almost, spherical, with the helices forming the external coat. There is a large, hydrophilic cavity in the center with open ends along the 5-fold axis., Molecular interactions between subunits are extensive. Each subunit, contacts four neighbors and loses nearly 40% of its solvent contact area, on oligomerization.
The crystal structure of muconolactone isomerase from Pseudomonas putida, a unique molecule with ten 96 amino acid subunits and 5-fold, and 2-fold symmetries, has been solved at 3.3 A resolution. The non-crystallographic symmetries were used to refine the initial single isomorphous replacement phases and produce an interpretable 10-fold averaged map. The backbone trace is complete and confirmed by the amino acid sequence fit. Each subunit is composed of a body with two alpha-helices and an antiparallel twisted beta-sheet of four strands, and an extended arm. The helices and the sheet fold to form a two-layered structure with an enclosed hydrophobic core and a partially formed putative active site pocket. The C-terminal arm of another subunit related by a local dyad symmetry extends over the core to complete this pocket. The decameric protein is almost spherical, with the helices forming the external coat. There is a large hydrophilic cavity in the center with open ends along the 5-fold axis. Molecular interactions between subunits are extensive. Each subunit contacts four neighbors and loses nearly 40% of its solvent contact area on oligomerization.


==About this Structure==
==About this Structure==
1MLI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Active as [http://en.wikipedia.org/wiki/Muconolactone_Delta-isomerase Muconolactone Delta-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.3.4 5.3.3.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MLI OCA].  
1MLI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Active as [http://en.wikipedia.org/wiki/Muconolactone_Delta-isomerase Muconolactone Delta-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.3.4 5.3.3.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MLI OCA].  


==Reference==
==Reference==
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[[Category: Pseudomonas putida]]
[[Category: Pseudomonas putida]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Katti, S.K.]]
[[Category: Katti, S K.]]
[[Category: Katz, B.A.]]
[[Category: Katz, B A.]]
[[Category: Wyckoff, H.W.]]
[[Category: Wyckoff, H W.]]
[[Category: intramolecular oxidoreductase]]
[[Category: intramolecular oxidoreductase]]


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