3fca

<table><tr><td colspan='2'>[[3fca]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FCA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FCA FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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=HQA:3-(8-HYDROXYQUINOLIN-3-YL)-L-ALANINE'>HQA</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cysteine_synthase Cysteine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.47 2.5.1.47] </span></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=3fca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fca OCA], [http://pdbe.org/3fca PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fca RCSB], [http://www.ebi.ac.uk/pdbsum/3fca PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3fca ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

A metal-ion chelating amino acid, (8-hydroxyquinolin-3-yl)alanine, was genetically encoded in E. coli by an amber nonsense codon and corresponding orthogonal tRNA/aminoacyl-tRNA synthetase pair. The amino acid was incorporated into TM0665 protein, and the mutant protein was cocrystallized with Zn(2+) to determine the structure by SAD phasing. The structure showed a high occupancy of the heavy metal bound to the HQ-Ala residue, and the heavy metal provided excellent phasing power to determine the structure. This method also facilitates the de novo design of metalloproteins with novel structures and functions, including fluorescent sensors.

Genetic Incorporation of a Metal-Ion Chelating Amino Acid into Proteins as a Biophysical Probe.,Lee HS, Spraggon G, Schultz PG, Wang F J Am Chem Soc. 2009 Feb 4. PMID:19193005<ref>PMID:19193005</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 3fca" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Flavobacterium thermophilum yoshida and oshima 1971]]

[[Category: Cysteine synthase]]

[[Category: Lee, H]]

[[Category: Schultz, P G]]

[[Category: Spraggon, G]]

[[Category: Wang, F]]

[[Category: Unnatural amino acid]]