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1jcd

From Proteopedia

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{{Seed}}
 
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[[Image:1jcd.png|left|200px]]
 
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==Crystal Structure of a Novel Alanine-Zipper Trimer at 1.3 A Resolution, I6A,L9A,V13A,L16A,V20A,L23A,V27A,M30A,V34A,L48A,M51A mutations==
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The line below this paragraph, containing "STRUCTURE_1jcd", creates the "Structure Box" on the page.
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<StructureSection load='1jcd' size='340' side='right'caption='[[1jcd]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1jcd]] is a 3 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=1JCD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JCD FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jcd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jcd OCA], [https://pdbe.org/1jcd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jcd RCSB], [https://www.ebi.ac.uk/pdbsum/1jcd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jcd ProSAT]</span></td></tr>
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{{STRUCTURE_1jcd| PDB=1jcd | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LPP_ECOLI LPP_ECOLI] Interacts with the peptidoglycan both covalently and noncovalently. This interaction contributes to the maintenance of the structural and functional integrity of the cell envelope.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jc/1jcd_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1jcd ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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A major challenge in protein folding is to identify and quantify specific structural determinants that allow native proteins to acquire their unique folded structures. Here we report the engineering of a 52-residue protein (Ala-14) that contains exclusively alanine residues at the hydrophobic a and d positions of a natural heptad-repeat sequence. Ala-14 is unfolded under normal solution conditions yet forms a parallel three-stranded alpha-helical coiled coil in crystals. Ala-14 trimers in the solid state associate with each other through the pairing of polar side chains and formation of an extended network of water-mediated hydrogen bonds. In contrast to the classical view that local intramolecular tertiary interactions dictate the three-dimensional structure of small single-domain proteins, Ala-14 shows that long range intermolecular interactions can be essential in determining the metastable alanine-zipper structure. A similar interplay between short range local and longer range global forces may underlie the conformational properties of the growing class of natively unstructured proteins in biological processes.
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===Crystal Structure of a Novel Alanine-Zipper Trimer at 1.3 A Resolution, I6A,L9A,V13A,L16A,V20A,L23A,V27A,M30A,V34A,L48A,M51A mutations===
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An alanine-zipper structure determined by long range intermolecular interactions.,Liu J, Lu M J Biol Chem. 2002 Dec 13;277(50):48708-13. Epub 2002 Oct 3. PMID:12368282<ref>PMID:12368282</ref>
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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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The line below this paragraph, {{ABSTRACT_PUBMED_12368282}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1jcd" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 12368282 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12368282}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1JCD is a 3 chains structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JCD OCA].
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==Reference==
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<ref group="xtra">PMID:12368282</ref><references group="xtra"/>
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Liu, J.]]
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[[Category: Large Structures]]
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[[Category: Lu, M.]]
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[[Category: Liu J]]
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[[Category: Alanine-zipper]]
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[[Category: Lu M]]
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[[Category: Coiled coil]]
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[[Category: Helix capping]]
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[[Category: Lipoprotein]]
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[[Category: Protein folding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 20:45:27 2009''
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Current revision

Crystal Structure of a Novel Alanine-Zipper Trimer at 1.3 A Resolution, I6A,L9A,V13A,L16A,V20A,L23A,V27A,M30A,V34A,L48A,M51A mutations

PDB ID 1jcd

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