4u9d: Difference between revisions

Line 1:

'''~~Unreleased~~ structure'''

==Crystal Structure of the Zn-directed tetramer of the engineered cyt cb562 variant, AB3==

== Structural highlights ==

<table><tr><td colspan='2'>[[4u9d]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U9D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4U9D FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4u9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u9d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4u9d RCSB], [http://www.ebi.ac.uk/pdbsum/4u9d PDBsum]</span></td></tr>

</table>

== Function ==

[[http://www.uniprot.org/uniprot/C562_ECOLX C562_ECOLX]] Electron-transport protein of unknown function.

== Publication Abstract from PubMed ==

The generation of new enzymatic activities has mainly relied on repurposing the interiors of preexisting protein folds because of the challenge in designing functional, three-dimensional protein structures from first principles. Here we report an artificial metallo-beta-lactamase, constructed via the self-assembly of a structurally and functionally unrelated, monomeric redox protein into a tetrameric assembly that possesses catalytic zinc sites in its interfaces. The designed metallo-beta-lactamase is functional in the Escherichia coli periplasm and enables the bacteria to survive treatment with ampicillin. In vivo screening of libraries has yielded a variant that displays a catalytic proficiency [(k(cat)/K(m))/k(uncat)] for ampicillin hydrolysis of 2.3 x 10(6) and features the emergence of a highly mobile loop near the active site, a key component of natural beta-lactamases to enable substrate interactions.

~~The entry 4u9d is ON HOLD until Paper Publication~~

A designed supramolecular protein assembly with in vivo enzymatic activity.,Song WJ, Tezcan FA Science. 2014 Dec 19;346(6216):1525-8. doi: 10.1126/science.1259680. PMID:25525249<ref>PMID:25525249</ref>

~~Authors: Tezcan~~, F.A.~~, Song, W.J~~.

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

~~Description:~~

== References ==

[[Category: ~~Unreleased Structures~~]]

[[Category: Tezcan, F.A]]

__TOC__

[[Category: ~~Song, W.J~~]]

</StructureSection>

[[Category: Song, W J]]

[[Category: Tezcan, F A]]

[[Category: Designed enzyme]]

[[Category: Tetramer assembly]]

[[Category: Zn-coordinating protein]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==Crystal Structure of the Zn-directed tetramer of the engineered cyt cb562 variant, AB3==
+<StructureSection load='4u9d' size='340' side='right' caption='[[4u9d]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4u9d]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U9D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4U9D FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4u9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u9d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4u9d RCSB], [http://www.ebi.ac.uk/pdbsum/4u9d PDBsum]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/C562_ECOLX C562_ECOLX]] Electron-transport protein of unknown function.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The generation of new enzymatic activities has mainly relied on repurposing the interiors of preexisting protein folds because of the challenge in designing functional, three-dimensional protein structures from first principles. Here we report an artificial metallo-beta-lactamase, constructed via the self-assembly of a structurally and functionally unrelated, monomeric redox protein into a tetrameric assembly that possesses catalytic zinc sites in its interfaces. The designed metallo-beta-lactamase is functional in the Escherichia coli periplasm and enables the bacteria to survive treatment with ampicillin. In vivo screening of libraries has yielded a variant that displays a catalytic proficiency [(k(cat)/K(m))/k(uncat)] for ampicillin hydrolysis of 2.3 x 10(6) and features the emergence of a highly mobile loop near the active site, a key component of natural beta-lactamases to enable substrate interactions.
-The entry 4u9d is ON HOLD  until Paper Publication
+A designed supramolecular protein assembly with in vivo enzymatic activity.,Song WJ, Tezcan FA Science. 2014 Dec 19;346(6216):1525-8. doi: 10.1126/science.1259680. PMID:25525249<ref>PMID:25525249</ref>
-Authors: Tezcan, F.A., Song, W.J.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description:
+== References ==
-[[Category: Unreleased Structures]]
+<references/>
-[[Category: Tezcan, F.A]]
+__TOC__
-[[Category: Song, W.J]]
+</StructureSection>
+[[Category: Song, W J]]
+[[Category: Tezcan, F A]]
+[[Category: Designed enzyme]]
+[[Category: Tetramer assembly]]
+[[Category: Zn-coordinating protein]]