1fh1

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{{Seed}}
 
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[[Image:1fh1.png|left|200px]]
 
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<!--
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==BACKBONE FOLD OF NODF==
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The line below this paragraph, containing "STRUCTURE_1fh1", creates the "Structure Box" on the page.
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<StructureSection load='1fh1' size='340' side='right'caption='[[1fh1]]' 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'>[[1fh1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhizobium_leguminosarum Rhizobium leguminosarum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FH1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FH1 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">Solution NMR</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=1fh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fh1 OCA], [https://pdbe.org/1fh1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fh1 RCSB], [https://www.ebi.ac.uk/pdbsum/1fh1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fh1 ProSAT]</span></td></tr>
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{{STRUCTURE_1fh1| PDB=1fh1 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/NODF_RHILV NODF_RHILV] Proposed to synthesize nod factor fatty acyl chain. Involved in trans-2,trans-4,trans-6,cis-11-octadecatetraenoic acid biosynthesis.
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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/fh/1fh1_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=1fh1 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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Over the next few years, various genome projects will sequence many new genes and yield many new gene products. Many of these products will have no known function and little, if any, sequence homology to existing proteins. There is reason to believe that a rapid determination of a protein fold, even at low resolution, can aid in the identification of function and expedite the determination of structure at higher resolution. Recently devised NMR methods of measuring residual dipolar couplings provide one route to the determination of a fold. They do this by allowing the alignment of previously identified secondary structural elements with respect to each other. When combined with constraints involving loops connecting elements or other short-range experimental distance information, a fold is produced. We illustrate this approach to protein fold determination on (15)N-labeled Eschericia coli acyl carrier protein using a limited set of (15)N-(1)H and (1)H-(1)H dipolar couplings. We also illustrate an approach using a more extended set of heteronuclear couplings on a related protein, (13)C, (15)N-labeled NodF protein from Rhizobium leguminosarum.
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===BACKBONE FOLD OF NODF===
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Rapid determination of protein folds using residual dipolar couplings.,Fowler CA, Tian F, Al-Hashimi HM, Prestegard JH J Mol Biol. 2000 Dec 1;304(3):447-60. PMID:11090286<ref>PMID:11090286</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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<div class="pdbe-citations 1fh1" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_11090286}}, adds the Publication Abstract to the page
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*[[NodS|NodS]]
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(as it appears on PubMed at http://www.pubmed.gov), where 11090286 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11090286}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1FH1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rhizobium_leguminosarum Rhizobium leguminosarum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FH1 OCA].
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==Reference==
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Rapid determination of protein folds using residual dipolar couplings., Fowler CA, Tian F, Al-Hashimi HM, Prestegard JH, J Mol Biol. 2000 Dec 1;304(3):447-60. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11090286 11090286]
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[[Category: Rhizobium leguminosarum]]
[[Category: Rhizobium leguminosarum]]
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[[Category: Single protein]]
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[[Category: Al-Hashimi HM]]
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[[Category: Al-Hashimi, H M.]]
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[[Category: Fowler CA]]
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[[Category: Fowler, C A.]]
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[[Category: Prestegard JH]]
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[[Category: Prestegard, J H.]]
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[[Category: Tian F]]
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[[Category: Tian, F.]]
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[[Category: Protein backbone fold]]
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[[Category: Root nodulation factor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:14:14 2008''
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Current revision

BACKBONE FOLD OF NODF

PDB ID 1fh1

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