View source for 1jml


==Conversion of Monomeric Protein L to an Obligate Dimer by Computational Protein Design==
<StructureSection load='1jml' size='340' side='right'caption='[[1jml]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1jml]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Finegoldia_magna_ATCC_29328 Finegoldia magna ATCC 29328]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JML OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JML 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=1jml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jml OCA], [https://pdbe.org/1jml PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jml RCSB], [https://www.ebi.ac.uk/pdbsum/1jml PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jml ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q51912_FINMA Q51912_FINMA] 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jm/1jml_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jml ConSurf].
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== Publication Abstract from PubMed ==
Protein L consists of a single alpha-helix packed on a four-stranded beta-sheet formed by two symmetrically opposed beta-hairpins. We use a computer-based protein design procedure to stabilize a domain-swapped dimer of protein L in which the second beta-turn straightens and the C-terminal strand inserts into the beta-sheet of the partner. The designed obligate dimer contains three mutations (A52V, N53P, and G55A) and has a dissociation constant of approximately 700 pM, which is comparable to the dissociation constant of many naturally occurring protein dimers. The structure of the dimer has been determined by x-ray crystallography and is close to the in silico model.

Conversion of monomeric protein L to an obligate dimer by computational protein design.,Kuhlman B, O'Neill JW, Kim DE, Zhang KY, Baker D Proc Natl Acad Sci U S A. 2001 Sep 11;98(19):10687-91. Epub 2001 Aug 28. PMID:11526208<ref>PMID:11526208</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 1jml" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Finegoldia magna ATCC 29328]]
[[Category: Large Structures]]
[[Category: Baker D]]
[[Category: Kim DE]]
[[Category: Kuhlman B]]
[[Category: O'Neill JW]]
[[Category: Zhang KYJ]]