1jog: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
Line 3: Line 3:
<StructureSection load='1jog' size='340' side='right'caption='[[1jog]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='1jog' size='340' side='right'caption='[[1jog]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1jog]] is a 4 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=1JOG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1JOG FirstGlance]. <br>
<table><tr><td colspan='2'>[[1jog]] is a 4 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=1JOG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JOG FirstGlance]. <br>
</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>
</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HI0074 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 "Bacterium influenzae" Lehmann and Neumann 1896])</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></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=1jog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jog OCA], [http://pdbe.org/1jog PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jog RCSB], [http://www.ebi.ac.uk/pdbsum/1jog PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jog 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=1jog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jog OCA], [https://pdbe.org/1jog PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jog RCSB], [https://www.ebi.ac.uk/pdbsum/1jog PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jog ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HEPT_HAEIN HEPT_HAEIN] Probable toxic component of a type VII toxin-antitoxin (TA) system, probably an RNase. Neutralized by cognate antitoxin MntA. Neutralization is probably due to AMPylation by MntA (Probable). A mixture of HepT and MntA binds nucleotides; the highest affinity is for TTP, ATP binds more tightly than ADP or AMP (PubMed:16028221).<ref>PMID:16028221</ref> <ref>PMID:29555683</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 18: Line 20:
</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=1jog ConSurf].
</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=1jog ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of HI0074 from Haemophilus influenzae, a protein of unknown function, has been determined at a resolution of 2.4 A. The molecules form an up-down, four-helix bundle, and associate into homodimers. The fold is most closely related to the substrate-binding domain of KNTase, yet the amino acid sequences of the two proteins exhibit no significant homology. Sequence analyses of completely and incompletely sequenced genomes reveal that the two adjacent genes, HI0074 and HI0073, and their close relatives comprise a new family of nucleotidyltransferases, with 15 members at the time of writing. The analyses also indicate that this is one of eight families of a large nucleotidyltransferase superfamily, whose members were identified based on the proximity of the nucleotide- and substrate-binding domains on the respective genomes. Both HI0073 and HI0074 were annotated "hypothetical" in the original genome sequencing publication. HI0073 was cloned, expressed, and purified, and was shown to form a complex with HI0074 by polyacrylamide gel electrophoresis under nondenaturing conditions, analytic size exclusion chromatography, and dynamic light scattering. Double- and single-stranded DNA binding assays showed no evidence of DNA binding to HI0074 or to HI0073/HI0074 complex despite the suggestive shape of the putative binding cleft formed by the HI0074 dimer.
The HI0073/HI0074 protein pair from Haemophilus influenzae is a member of a new nucleotidyltransferase family: structure, sequence analyses, and solution studies.,Lehmann C, Lim K, Chalamasetty VR, Krajewski W, Melamud E, Galkin A, Howard A, Kelman Z, Reddy PT, Murzin AG, Herzberg O Proteins. 2003 Feb 1;50(2):249-60. PMID:12486719<ref>PMID:12486719</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1jog" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacterium influenzae lehmann and neumann 1896]]
[[Category: Haemophilus influenzae]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Herzberg, O]]
[[Category: Herzberg O]]
[[Category: Lehmann, C]]
[[Category: Lehmann C]]
[[Category: Lim, K]]
[[Category: Lim K]]
[[Category: S2F, Structure 2.Function Project]]
[[Category: Hi0074]]
[[Category: Hypothetical protein]]
[[Category: S2f]]
[[Category: Structural genomic]]
[[Category: Structure 2 function project]]
[[Category: Unknown function]]

Revision as of 07:53, 3 April 2024

Structure of HI0074 from Heamophilus Influenzae reveals the fold of a substrate binding domain of a nucleotidyltransferase

1jog, resolution 2.40Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1jog&oldid=4121155"