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1nla

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[[Image:1nla.png|left|200px]]
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==Solution Structure of Switch Arc, a Mutant with 3(10) Helices Replacing a Wild-Type Beta-Ribbon==
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<StructureSection load='1nla' size='340' side='right' caption='[[1nla]], [[NMR_Ensembles_of_Models | 13 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1nla]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p22 Enterobacteria phage p22]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NLA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NLA FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qtg|1qtg]]</td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ARC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10754 Enterobacteria phage P22])</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nla FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nla OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1nla RCSB], [http://www.ebi.ac.uk/pdbsum/1nla PDBsum]</span></td></tr>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Adjacent N11L and L12N mutations in the antiparallel beta-ribbon of Arc repressor result in dramatic changes in local structure in which each beta-strand is replaced by a right-handed helix. The full solution structure of this "switch" Arc mutant shows that irregular 3(10) helices compose the new secondary structure. This structural metamorphosis conserves the number of main-chain and side-chain to main-chain hydrogen bonds and the number of fully buried core residues. Apart from a slight widening of the interhelical angle between alpha-helices A and B and changes in side-chain conformation of a few core residues in Arc, no large-scale structural adjustments in the remainder of the protein are necessary to accommodate the ribbon-to-helix change. Nevertheless, some changes in hydrogen-exchange rates are observed, even in regions that have very similar structures in the two proteins. The surface of switch Arc is packed poorly compared to wild-type, leading to approximately 1000A(2) of additional solvent-accessible surface area, and the N termini of the 3(10) helices make unfavorable head-to-head electrostatic interactions. These structural features account for the positive m value and salt dependence of the ribbon-to-helix transition in Arc-N11L, a variant that can adopt either the mutant or wild-type structures. The tertiary fold is capped in different ways in switch and wild-type Arc, showing how stepwise evolutionary transformations can arise through small changes in amino acid sequence.
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{{STRUCTURE_1nla| PDB=1nla | SCENE= }}
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Solution structure of switch Arc, a mutant with 3(10) helices replacing a wild-type beta-ribbon.,Cordes MH, Walsh NP, McKnight CJ, Sauer RT J Mol Biol. 2003 Feb 21;326(3):899-909. PMID:12581649<ref>PMID:12581649</ref>
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===Solution Structure of Switch Arc, a Mutant with 3(10) Helices Replacing a Wild-Type Beta-Ribbon===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_12581649}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[1nla]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p22 Enterobacteria phage p22]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NLA OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:012581649</ref><references group="xtra"/>
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[[Category: Enterobacteria phage p22]]
[[Category: Enterobacteria phage p22]]
[[Category: Cordes, M H.]]
[[Category: Cordes, M H.]]

Revision as of 06:56, 9 June 2014

Solution Structure of Switch Arc, a Mutant with 3(10) Helices Replacing a Wild-Type Beta-Ribbon

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