1fh1: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| (17 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
== | ==BACKBONE FOLD OF NODF== | ||
<StructureSection load='1fh1' size='340' side='right'caption='[[1fh1]]' scene=''> | |||
== Structural highlights == | |||
<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> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=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> | |||
</table> | |||
== Function == | |||
[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. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fh/1fh1_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | 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. | ||
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> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
<div class="pdbe-citations 1fh1" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[NodS|NodS]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Rhizobium leguminosarum]] | [[Category: Rhizobium leguminosarum]] | ||
[[Category: Al-Hashimi HM]] | |||
[[Category: Al-Hashimi | [[Category: Fowler CA]] | ||
[[Category: Fowler | [[Category: Prestegard JH]] | ||
[[Category: Prestegard | [[Category: Tian F]] | ||
[[Category: Tian | |||
Latest revision as of 11:28, 22 May 2024
BACKBONE FOLD OF NODFBACKBONE FOLD OF NODF
Structural highlights
FunctionNODF_RHILV Proposed to synthesize nod factor fatty acyl chain. Involved in trans-2,trans-4,trans-6,cis-11-octadecatetraenoic acid biosynthesis. 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 PubMedOver 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||