View source for 3tol


==Crystal structure of an engineered cytochrome cb562 that forms 1D, Zn-mediated coordination polymers==
<StructureSection load='3tol' size='340' side='right'caption='[[3tol]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3tol]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TOL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TOL FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <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'>[https://proteopedia.org/fgij/fg.htm?mol=3tol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tol OCA], [https://pdbe.org/3tol PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tol RCSB], [https://www.ebi.ac.uk/pdbsum/3tol PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tol ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/C562_ECOLX C562_ECOLX] Electron-transport protein of unknown function.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Proteins represent the most sophisticated building blocks available to an organism and to the laboratory chemist. Yet, in contrast to nearly all other types of molecular building blocks, the designed self-assembly of proteins has largely been inaccessible because of the chemical and structural heterogeneity of protein surfaces. To circumvent the challenge of programming extensive non-covalent interactions to control protein self-assembly, we have previously exploited the directionality and strength of metal coordination interactions to guide the formation of closed, homoligomeric protein assemblies. Here, we extend this strategy to the generation of periodic protein arrays. We show that a monomeric protein with properly oriented coordination motifs on its surface can arrange, on metal binding, into one-dimensional nanotubes and two- or three-dimensional crystalline arrays with dimensions that collectively span nearly the entire nano- and micrometre scale. The assembly of these arrays is tuned predictably by external stimuli, such as metal concentration and pH.

Metal-directed, chemically tunable assembly of one-, two- and three-dimensional crystalline protein arrays.,Brodin JD, Ambroggio XI, Tang C, Parent KN, Baker TS, Tezcan FA Nat Chem. 2012 Mar 4;4(5):375-82. doi: 10.1038/nchem.1290. PMID:22522257<ref>PMID:22522257</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3tol" style="background-color:#fffaf0;"></div>

==See Also==
*[[Cytochrome b5 3D structures|Cytochrome b5 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Brodin JB]]
[[Category: Tezcan FA]]