2p74: Difference between revisions

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New page: left|200px<br /><applet load="2p74" size="350" color="white" frame="true" align="right" spinBox="true" caption="2p74, resolution 0.88Å" /> '''CTX-M-9 class A beta...
 
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caption="2p74, resolution 0.88&Aring;" />
caption="2p74, resolution 0.88&Aring;" />
'''CTX-M-9 class A beta-lactamase apo crystal structure at 0.88 Angstrom resolution'''<br />
'''CTX-M-9 class A beta-lactamase apo crystal structure at 0.88 Angstrom resolution'''<br />
==Overview==
The apo crystal structure of CTX-M-9 beta-lactamase has been determined to, 0.88 A at pH 8.8. This unusually clear picture of proton positions and, residue interactions supports the role of Glu166 as the general base for, the controversial acylation step of class A beta-lactamase catalysis. The, ability to distinguish low-energy conformations sampled by the enzyme, allows us to link the two conformations of Lys73 to different protonation, states of Glu166.


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
The Acylation Mechanism of CTX-M beta-Lactamase at 0.88 A Resolution., Chen Y, Bonnet R, Shoichet BK, J Am Chem Soc. 2007 Apr 5;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17408273 17408273]
The acylation mechanism of CTX-M beta-lactamase at 0.88 a resolution., Chen Y, Bonnet R, Shoichet BK, J Am Chem Soc. 2007 May 2;129(17):5378-80. Epub 2007 Apr 5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17408273 17408273]
[[Category: Beta-lactamase]]
[[Category: Beta-lactamase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Bonnet, R.]]
[[Category: Bonnet, R.]]
[[Category: Chen, Y.]]
[[Category: Chen, Y.]]
[[Category: Shoichet, B.K.]]
[[Category: Shoichet, B K.]]
[[Category: K]]
[[Category: K]]
[[Category: PO4]]
[[Category: PO4]]
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[[Category: ultra-high resolution]]
[[Category: ultra-high resolution]]


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