1xnf

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{{Seed}}
 
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[[Image:1xnf.png|left|200px]]
 
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==Crystal structure of E.coli TPR-protein NlpI==
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The line below this paragraph, containing "STRUCTURE_1xnf", creates the "Structure Box" on the page.
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<StructureSection load='1xnf' size='340' side='right'caption='[[1xnf]], [[Resolution|resolution]] 1.98&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'>[[1xnf]] is a 2 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=1XNF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XNF 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]] 1.98&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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{{STRUCTURE_1xnf| PDB=1xnf | SCENE= }}
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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=1xnf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xnf OCA], [https://pdbe.org/1xnf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xnf RCSB], [https://www.ebi.ac.uk/pdbsum/1xnf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xnf ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/NLPI_ECOLI NLPI_ECOLI] May be involved in cell division. May play a role in bacterial septation or regulation of cell wall degradation during cell division. Negatively controls the production of extracellular DNA (eDNA).<ref>PMID:10400590</ref> <ref>PMID:20833130</ref>
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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/xn/1xnf_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1xnf 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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There are several different families of repeat proteins. In each, a distinct structural motif is repeated in tandem to generate an elongated structure. The nonglobular, extended structures that result are particularly well suited to present a large surface area and to function as interaction domains. Many repeat proteins have been demonstrated experimentally to fold and function as independent domains. In tetratricopeptide (TPR) repeats, the repeat unit is a helix-turn-helix motif. The majority of TPR motifs occur as three to over 12 tandem repeats in different proteins. The majority of TPR structures in the Protein Data Bank are of isolated domains. Here we present the high-resolution structure of NlpI, the first structure of a complete TPR-containing protein. We show that in this instance the TPR motifs do not fold and function as an independent domain, but are fully integrated into the three-dimensional structure of a globular protein. The NlpI structure is also the first TPR structure from a prokaryote. It is of particular interest because it is a membrane-associated protein, and mutations in it alter septation and virulence.
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===Crystal structure of E.coli TPR-protein NlpI===
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The crystal structure of NlpI. A prokaryotic tetratricopeptide repeat protein with a globular fold.,Wilson CG, Kajander T, Regan L FEBS J. 2005 Jan;272(1):166-79. PMID:15634341<ref>PMID:15634341</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_15634341}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1xnf" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 15634341 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15634341}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1XNF is a [[Single protein]] structure of sequence 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=1XNF OCA].
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==Reference==
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The crystal structure of NlpI. A prokaryotic tetratricopeptide repeat protein with a globular fold., Wilson CG, Kajander T, Regan L, FEBS J. 2005 Jan;272(1):166-79. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15634341 15634341]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Kajander, T.]]
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[[Category: Kajander T]]
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[[Category: Regan, L.]]
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[[Category: Regan L]]
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[[Category: Wilson, C G.]]
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[[Category: Wilson CG]]
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[[Category: Lipoprotein]]
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[[Category: Nlpi]]
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[[Category: Structural genomic]]
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[[Category: Tetratricopeptide]]
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[[Category: Tpr]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:21:15 2008''
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Current revision

Crystal structure of E.coli TPR-protein NlpI

PDB ID 1xnf

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