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1jog

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[[Image:1jog.jpg|left|200px]]<br /><applet load="1jog" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1jog, resolution 2.4&Aring;" />
 
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'''Structure of HI0074 from Heamophilus Influenzae reveals the fold of a substrate binding domain of a nucleotidyltransferase'''<br />
 
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==Overview==
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==Structure of HI0074 from Heamophilus Influenzae reveals the fold of a substrate binding domain of a nucleotidyltransferase==
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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.
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<StructureSection load='1jog' size='340' side='right'caption='[[1jog]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<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>
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1JOG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://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].
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</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>
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<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>
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==Reference==
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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=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>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12486719 12486719]
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</table>
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== Function ==
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[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>
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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/jo/1jog_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=1jog ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Haemophilus influenzae]]
[[Category: Haemophilus influenzae]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Herzberg, O.]]
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[[Category: Herzberg O]]
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[[Category: Lehmann, C.]]
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[[Category: Lehmann C]]
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[[Category: Lim, K.]]
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[[Category: Lim K]]
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[[Category: S2F, Structure 2.Function Project.]]
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[[Category: hi0074]]
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[[Category: hypothetical protein]]
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[[Category: s2f]]
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[[Category: structural genomics]]
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[[Category: structure 2 function project]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:24:54 2008''
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Current revision

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

PDB ID 1jog

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