View source for 4zgl


==Hit Like Protein==
<StructureSection load='4zgl' size='340' side='right'caption='[[4zgl]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4zgl]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4q61 4q61]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZGL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZGL FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.95&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene></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=4zgl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zgl OCA], [https://pdbe.org/4zgl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zgl RCSB], [https://www.ebi.ac.uk/pdbsum/4zgl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zgl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/YHIT_HELPY YHIT_HELPY] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Proteins belonging to the histidine triad (HIT) superfamily bind nucleotides and use the histidine triad motif to carry out dinucleotidyl hydrolase, nucleotidyltransferase and phosphoramidite hydrolase activities. Five different branches of this superfamily are known to exist. Defects in these proteins in humans are linked to many diseases such as ataxia, diseases of RNA metabolism and cell-cycle regulation, and various types of cancer. The histidine triad nucleotide protein (HINT) is nearly identical to proteins that have been classified as protein kinase C-interacting proteins (PKCIs), which also have the ability to bind and inhibit protein kinase C. The structure of HINT, which exists as a homodimer, is highly conserved from humans to bacteria and shares homology with the product of fragile histidine triad protein (FHit), a tumour suppressor gene of this superfamily. Here, the structure of HINT from Helicobacter pylori (HpHINT) in complex with AMP is reported at a resolution of 3 A. The final model has R and Rfree values of 26 and 28%, respectively, with good electron density. Structural comparison with previously reported homologues and phylogenetic analysis shows H. pylori HINT to be the smallest among them, and suggests that it branched out separately during the course of evolution. Overall, this structure has contributed to a better understanding of this protein across the animal kingdom.

Crystal structure of HINT from Helicobacter pylori.,Tarique KF, Devi S, Abdul Rehman SA, Gourinath S Acta Crystallogr F Struct Biol Commun. 2016 Jan;72(Pt 1):42-8. doi:, 10.1107/S2053230X15023316. Epub 2016 Jan 1. PMID:26750483<ref>PMID:26750483</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4zgl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Helicobacter pylori 26695]]
[[Category: Large Structures]]
[[Category: Abdul Rehman SA]]
[[Category: Devi S]]
[[Category: Gourinath S]]
[[Category: Tarique KF]]