3pbj

<table><tr><td colspan='2'>[[3pbj]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PBJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PBJ FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=LE1:3-SULFANYL-L-VALINE'>LE1</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3h5f|3h5f]], [[3h5g|3h5g]], [[2jgo|2jgo]], [[3ljm|3ljm]], [[2x6p|2x6p]]</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=3pbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pbj OCA], [http://pdbe.org/3pbj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3pbj RCSB], [http://www.ebi.ac.uk/pdbsum/3pbj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3pbj ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Metal ions are an important part of many natural proteins, providing structural, catalytic and electron transfer functions. Reproducing these functions in a designed protein is the ultimate challenge to our understanding of them. Here, we present an artificial metallohydrolase, which has been shown by X-ray crystallography to contain two different metal ions-a Zn(II) ion, which is important for catalytic activity, and a Hg(II) ion, which provides structural stability. This metallohydrolase displays catalytic activity that compares well with several characteristic reactions of natural enzymes. It catalyses p-nitrophenyl acetate (pNPA) hydrolysis with an efficiency only ~100-fold less than that of human carbonic anhydrase (CA)II and at least 550-fold better than comparable synthetic complexes. Similarly, CO(2) hydration occurs with an efficiency within ~500-fold of CAII. Although histidine residues in the absence of Zn(II) exhibit pNPA hydrolysis, miniscule apopeptide activity is observed for CO(2) hydration. The kinetic and structural analysis of this first de novo designed hydrolytic metalloenzyme reveals necessary design features for future metalloenzymes containing one or more metals.

Hydrolytic catalysis and structural stabilization in a designed metalloprotein.,Zastrow ML, Peacock AF, Stuckey JA, Pecoraro VL Nat Chem. 2011 Nov 27;4(2):118-23. doi: 10.1038/nchem.1201. PMID:22270627<ref>PMID:22270627</ref>

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

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<div class="pdbe-citations 3pbj" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Peacock, A F.A]]

[[Category: Pecoraro, V L]]

[[Category: Stuckey, J A]]

[[Category: Zastrow, M L]]

[[Category: De novo protein]]

[[Category: Parallel three-stranded coiled coil]]