1jal: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 3: / Line 3: @@
 <StructureSection load='1jal' size='340' side='right'caption='[[1jal]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1jal]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_influenzae"_lehmann_and_neumann_1896 "bacterium influenzae" lehmann and neumann 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JAL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1JAL FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1jal]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JAL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JAL FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YchF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 "Bacterium influenzae" Lehmann and Neumann 1896])</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]] 2.4&#8491;</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=1jal FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jal OCA], [http://pdbe.org/1jal PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jal RCSB], [http://www.ebi.ac.uk/pdbsum/1jal PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jal ProSAT]</span></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=1jal FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jal OCA], [https://pdbe.org/1jal PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jal RCSB], [https://www.ebi.ac.uk/pdbsum/1jal PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jal ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/YCHF_HAEIN YCHF_HAEIN]] ATPase that binds to both the 70S ribosome and the 50S ribosomal subunit in a nucleotide-independent manner (By similarity). Does not hydrolyze GTP.[HAMAP-Rule:MF_00944]<ref>PMID:17430889</ref>
+[https://www.uniprot.org/uniprot/YCHF_HAEIN YCHF_HAEIN] ATPase that binds to both the 70S ribosome and the 50S ribosomal subunit in a nucleotide-independent manner (By similarity). Does not hydrolyze GTP.[HAMAP-Rule:MF_00944]<ref>PMID:17430889</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 19: / Line 19: @@
 </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=1jal ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The bacterial protein encoded by the gene ychF is 1 of 11 universally conserved GTPases and the only one whose function is unknown. The crystal structure determination of YchF was sought to help with the functional assignment of the protein. The YchF protein from Haemophilus influenzae was cloned and expressed, and the crystal structure was determined at 2.4 A resolution. The polypeptide chain is folded into three domains. The N-terminal domain has a mononucleotide binding fold typical for the P-loop NTPases. An 80-residue domain next to it has a pronounced alpha-helical coiled coil. The C-terminal domain features a six-stranded half-barrel that curves around an alpha-helix. The crablike three-domain structure of YchF suggests the binding site for a double-stranded nucleic acid in the cleft between the domains. The structure of the putative GTP-binding site is consistent with the postulated guanine specificity of the protein. Fluorescence measurements have demonstrated the ability of YchF to bind a double-stranded nucleic acid and GTP. Taken together with other experimental data and genomic analysis, these results suggest that YchF may be part of a nucleoprotein complex and may function as a GTP-dependent translation factor.
-Crystal structure of the YchF protein reveals binding sites for GTP and nucleic acid.,Teplyakov A, Obmolova G, Chu SY, Toedt J, Eisenstein E, Howard AJ, Gilliland GL J Bacteriol. 2003 Jul;185(14):4031-7. PMID:12837776<ref>PMID:12837776</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1jal" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Bacterium influenzae lehmann and neumann 1896]]
+[[Category: Haemophilus influenzae]]
 [[Category: Large Structures]]
-[[Category: Gilliland, G L]]
+[[Category: Gilliland GL]]
-[[Category: S2F, Structure 2.Function Project]]
+[[Category: Teplyakov A]]
-[[Category: Teplyakov, A]]
-[[Category: Nucleotide-binding fold]]
-[[Category: S2f]]
-[[Category: Structural genomic]]
-[[Category: Structure 2 function project]]
-[[Category: Unknown function]]