1m2x: Difference between revisions

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[[Image:1m2x.jpg|left|200px]]<br /><applet load="1m2x" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1m2x.jpg|left|200px]]<br /><applet load="1m2x" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1m2x, resolution 1.5Å" />

'''Crystal Structure of the metallo-beta-lactamase BlaB of Chryseobacterium meningosepticum in complex with the inhibitor D-captopril'''<br />

==Overview==

The crystal structure of the class-B beta-lactamase, BlaB, from the, pathogenic bacterium, Chryseobacterium meningosepticum, in complex with, the inhibitor, d-captopril, has been solved at 1.5-A resolution. The, enzyme has the typical alphabeta/betaalpha metallo-beta-lactamase fold and, the characteristic two metal binding sites of members of the subclass B1, in which two Zn2+ ions were identified. d-Captopril, a diastereoisomer of, the commercial drug, captopril, acts as an inhibitor by displacing the, catalytic hydroxyl ion required for antibiotic hydrolysis and, intercalating its sulfhydryl group between the two Zn2+ ions., Interestingly, d-captopril is located on one side of the active site, cleft. The x-ray structure of the complex of the closely related enzyme, IMP-1, with a mercaptocarboxylate inhibitor, which also contains a, sulfhydryl group bound to the two Zn2+ ions, shows the ligand to be, located on the opposite side of the active site cleft. A molecule, generated by fusion of these two inhibitors would cover the entire cleft, suggesting an interesting approach to the design of highly specific, inhibitors.

The crystal structure of the class-B beta-lactamase, BlaB, from the pathogenic bacterium, Chryseobacterium meningosepticum, in complex with the inhibitor, d-captopril, has been solved at 1.5-A resolution. The enzyme has the typical alphabeta/betaalpha metallo-beta-lactamase fold and the characteristic two metal binding sites of members of the subclass B1, in which two Zn2+ ions were identified. d-Captopril, a diastereoisomer of the commercial drug, captopril, acts as an inhibitor by displacing the catalytic hydroxyl ion required for antibiotic hydrolysis and intercalating its sulfhydryl group between the two Zn2+ ions. Interestingly, d-captopril is located on one side of the active site cleft. The x-ray structure of the complex of the closely related enzyme, IMP-1, with a mercaptocarboxylate inhibitor, which also contains a sulfhydryl group bound to the two Zn2+ ions, shows the ligand to be located on the opposite side of the active site cleft. A molecule generated by fusion of these two inhibitors would cover the entire cleft, suggesting an interesting approach to the design of highly specific inhibitors.

==About this Structure==

1M2X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Elizabethkingia_meningoseptica Elizabethkingia meningoseptica] with NA, ZN, MCO and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1M2X OCA].

1M2X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Elizabethkingia_meningoseptica Elizabethkingia meningoseptica] with <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=MCO:'>MCO</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M2X OCA].

==Reference==

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[[Category: alpha-beta/beta-alpha fold.]]

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@@ Line 1: / Line 1: @@
-[[Image:1m2x.jpg|left|200px]]<br /><applet load="1m2x" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1m2x.jpg|left|200px]]<br /><applet load="1m2x" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1m2x, resolution 1.5&Aring;" />
 '''Crystal Structure of the metallo-beta-lactamase BlaB of Chryseobacterium meningosepticum in complex with the inhibitor D-captopril'''<br />
 ==Overview==
-The crystal structure of the class-B beta-lactamase, BlaB, from the, pathogenic bacterium, Chryseobacterium meningosepticum, in complex with, the inhibitor, d-captopril, has been solved at 1.5-A resolution. The, enzyme has the typical alphabeta/betaalpha metallo-beta-lactamase fold and, the characteristic two metal binding sites of members of the subclass B1, in which two Zn2+ ions were identified. d-Captopril, a diastereoisomer of, the commercial drug, captopril, acts as an inhibitor by displacing the, catalytic hydroxyl ion required for antibiotic hydrolysis and, intercalating its sulfhydryl group between the two Zn2+ ions., Interestingly, d-captopril is located on one side of the active site, cleft. The x-ray structure of the complex of the closely related enzyme, IMP-1, with a mercaptocarboxylate inhibitor, which also contains a, sulfhydryl group bound to the two Zn2+ ions, shows the ligand to be, located on the opposite side of the active site cleft. A molecule, generated by fusion of these two inhibitors would cover the entire cleft, suggesting an interesting approach to the design of highly specific, inhibitors.
+The crystal structure of the class-B beta-lactamase, BlaB, from the pathogenic bacterium, Chryseobacterium meningosepticum, in complex with the inhibitor, d-captopril, has been solved at 1.5-A resolution. The enzyme has the typical alphabeta/betaalpha metallo-beta-lactamase fold and the characteristic two metal binding sites of members of the subclass B1, in which two Zn2+ ions were identified. d-Captopril, a diastereoisomer of the commercial drug, captopril, acts as an inhibitor by displacing the catalytic hydroxyl ion required for antibiotic hydrolysis and intercalating its sulfhydryl group between the two Zn2+ ions. Interestingly, d-captopril is located on one side of the active site cleft. The x-ray structure of the complex of the closely related enzyme, IMP-1, with a mercaptocarboxylate inhibitor, which also contains a sulfhydryl group bound to the two Zn2+ ions, shows the ligand to be located on the opposite side of the active site cleft. A molecule generated by fusion of these two inhibitors would cover the entire cleft, suggesting an interesting approach to the design of highly specific inhibitors.
 ==About this Structure==
-M2X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Elizabethkingia_meningoseptica Elizabethkingia meningoseptica] with NA, ZN, MCO and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M2X OCA].
+M2X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Elizabethkingia_meningoseptica Elizabethkingia meningoseptica] with <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=MCO:'>MCO</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M2X OCA].
 ==Reference==
@@ Line 22: / Line 22: @@
 [[Category: alpha-beta/beta-alpha fold.]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:06:16 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:50:54 2008''