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| | <StructureSection load='1xnf' size='340' side='right'caption='[[1xnf]], [[Resolution|resolution]] 1.98Å' scene=''> | | <StructureSection load='1xnf' size='340' side='right'caption='[[1xnf]], [[Resolution|resolution]] 1.98Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1xnf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1XNF FirstGlance]. <br> | + | <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> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.98Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <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> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nlpi ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1xnf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xnf OCA], [http://pdbe.org/1xnf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xnf RCSB], [http://www.ebi.ac.uk/pdbsum/1xnf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xnf ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> | + | [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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kajander, T]] | + | [[Category: Kajander T]] |
| - | [[Category: Regan, L]] | + | [[Category: Regan L]] |
| - | [[Category: Wilson, C G]] | + | [[Category: Wilson CG]] |
| - | [[Category: Lipoprotein]]
| + | |
| - | [[Category: Nlpi]]
| + | |
| - | [[Category: Structural genomic]]
| + | |
| - | [[Category: Tetratricopeptide]]
| + | |
| - | [[Category: Tpr]]
| + | |
| - | [[Category: Unknown function]]
| + | |
| Structural highlights
Function
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).[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ohara M, Wu HC, Sankaran K, Rick PD. Identification and characterization of a new lipoprotein, NlpI, in Escherichia coli K-12. J Bacteriol. 1999 Jul;181(14):4318-25. PMID:10400590
- ↑ Sanchez-Torres V, Maeda T, Wood TK. Global regulator H-NS and lipoprotein NlpI influence production of extracellular DNA in Escherichia coli. Biochem Biophys Res Commun. 2010 Oct 15;401(2):197-202. doi:, 10.1016/j.bbrc.2010.09.026. Epub 2010 Sep 15. PMID:20833130 doi:http://dx.doi.org/10.1016/j.bbrc.2010.09.026
- ↑ Wilson CG, Kajander T, Regan L. The crystal structure of NlpI. A prokaryotic tetratricopeptide repeat protein with a globular fold. FEBS J. 2005 Jan;272(1):166-79. PMID:15634341 doi:10.1111/j.1432-1033.2004.04397.x
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