View source for 2bni

==PLI MUTANT E20C L16G Y17H, ANTIPARALLEL==
<StructureSection load='2bni' size='340' side='right' caption='[[2bni]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2bni]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BNI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BNI FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TYZ:PARA+ACETAMIDO+BENZOIC+ACID'>TYZ</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ce9|1ce9]], [[1dgc|1dgc]], [[1env|1env]], [[1fav|1fav]], [[1gcl|1gcl]], [[1gcm|1gcm]], [[1gk6|1gk6]], [[1gzl|1gzl]], [[1ihq|1ihq]], [[1ij0|1ij0]], [[1ij1|1ij1]], [[1ij2|1ij2]], [[1ij3|1ij3]], [[1kql|1kql]], [[1ld4|1ld4]], [[1llm|1llm]], [[1nkn|1nkn]], [[1piq|1piq]], [[1rb1|1rb1]], [[1rb4|1rb4]], [[1rb5|1rb5]], [[1rb6|1rb6]], [[1swi|1swi]], [[1tmz|1tmz]], [[1unt|1unt]], [[1unu|1unu]], [[1unv|1unv]], [[1unw|1unw]], [[1unx|1unx]], [[1uny|1uny]], [[1unz|1unz]], [[1uo0|1uo0]], [[1uo1|1uo1]], [[1uo2|1uo2]], [[1uo3|1uo3]], [[1uo4|1uo4]], [[1uo5|1uo5]], [[1vzl|1vzl]], [[1w5g|1w5g]], [[1w5h|1w5h]], [[1w5i|1w5i]], [[1w5j|1w5j]], [[1w5k|1w5k]], [[1w5l|1w5l]], [[1ysa|1ysa]], [[1zii|1zii]], [[1zij|1zij]], [[1zik|1zik]], [[1zil|1zil]], [[1zim|1zim]], [[1zta|1zta]], [[2dgc|2dgc]], [[2zta|2zta]]</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=2bni FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bni OCA], [http://pdbe.org/2bni PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bni RCSB], [http://www.ebi.ac.uk/pdbsum/2bni PDBsum]</span></td></tr>
</table>
== 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/bn/2bni_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/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cavities and clefts are frequently important sites of interaction between natural enzymes or receptors and their corresponding substrate or ligand molecules and exemplify the types of molecular surfaces that would facilitate engineering of artificial catalysts and receptors. Even so, structural characterizations of designed cavities are rare. To address this issue, we performed a systematic study of the structural effects of single-amino acid substitutions within the hydrophobic cores of tetrameric coiled-coil peptides. Peptides containing single glycine, serine, alanine, or threonine amino acid substitutions at the buried L9, L16, L23, and I26 hydrophobic core positions of a GCN4-based sequence were synthesized and studied by solution-phase and crystallographic techniques. All peptides adopt the expected tetrameric state and contain tunnels or internal cavities ranging in size from 80 to 370 A(3). Two closely related sequences containing an L16G substitution, one of which adopts an antiparallel configuration and one of which adopts a parallel configuration, illustrate that cavities of different volumes and shapes can be engineered from identical core substitutions. Finally, we demonstrate that two of the peptides (L9G and L9A) bind the small molecule iodobenzene when present during crystallization, leaving the general peptide quaternary structure intact but altering the local peptide conformation and certain superhelical parameters. These high-resolution descriptions of varied molecular surfaces within solvent-occluded internal cavities illustrate the breadth of design space available in even closely related peptides and offer valuable models for the engineering of de novo helical proteins.

Structure-based engineering of internal cavities in coiled-coil peptides.,Yadav MK, Redman JE, Leman LJ, Alvarez-Gutierrez JM, Zhang Y, Stout CD, Ghadiri MR Biochemistry. 2005 Jul 19;44(28):9723-32. PMID:16008357<ref>PMID:16008357</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2bni" style="background-color:#fffaf0;"></div>

==See Also==
*[[Gcn4|Gcn4]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Ghadiri, M R]]
[[Category: Leman, L J]]
[[Category: Stout, C D]]
[[Category: Yadav, M K]]
[[Category: Antiparallel four helix bundle acyl transferase]]
[[Category: Four helix bundle]]