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[[Image:5rhn.gif|left|200px]]<br />
<applet load="5rhn" size="450" color="white" frame="true" align="right" spinBox="true"
caption="5rhn, resolution 2.31&Aring;" />
'''HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN (HINT) FROM RABBIT COMPLEXED WITH 8-BR-AMP'''<br />


==Overview==
==HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN (HINT) FROM RABBIT COMPLEXED WITH 8-BR-AMP==
Histidine triad nucleotide-binding protein (HINT), a dimeric purine, nucleotide-binding protein from rabbit heart, is a member of the HIT, (histidine triad) superfamily which includes HINT homologues and FHIT (HIT, protein encoded at the chromosome 3 fragile site) homologues. Crystal, structures of HINT-nucleotide complexes demonstrate that the most, conserved residues in the superfamily mediate nucleotide binding and that, the HIT motif forms part of the phosphate binding loop., Galactose-1-phosphate uridylyltransferase, whose deficiency causes, galactosemia, contains tandem HINT domains with the same fold and mode of, nucleotide binding as HINT despite having no overall sequence similarity., Features of FHIT, a diadenosine polyphosphate hydrolase and candidate, tumour suppressor, are predicted from HINT-nucleotide structures.
<StructureSection load='5rhn' size='340' side='right'caption='[[5rhn]], [[Resolution|resolution]] 2.31&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5rhn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5RHN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5RHN 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]] 2.31&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8BR:8-BROMO-ADENOSINE-5-MONOPHOSPHATE'>8BR</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=5rhn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5rhn OCA], [https://pdbe.org/5rhn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5rhn RCSB], [https://www.ebi.ac.uk/pdbsum/5rhn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5rhn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HINT1_RABIT HINT1_RABIT] Hydrolyzes adenosine 5'-monophosphoramidate substrates such as AMP-morpholidate, AMP-N-alanine methyl ester, AMP-alpha-acetyl lysine methyl ester and AMP-NH2.
== 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/rh/5rhn_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=5rhn ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
5RHN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with 8BR as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: HIT. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=5RHN OCA].
*[[Histidine triad nucleotide-binding protein 3D structures|Histidine triad nucleotide-binding protein 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Crystal structures of HINT demonstrate that histidine triad proteins are GalT-related nucleotide-binding proteins., Brenner C, Garrison P, Gilmour J, Peisach D, Ringe D, Petsko GA, Lowenstein JM, Nat Struct Biol. 1997 Mar;4(3):231-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9164465 9164465]
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Single protein]]
[[Category: Brenner C]]
[[Category: Brenner, C.]]
[[Category: Garrison P]]
[[Category: Garrison, P.]]
[[Category: Gilmour J]]
[[Category: Gilmour, J.]]
[[Category: Lowenstein JM]]
[[Category: Lowenstein, J.M.]]
[[Category: Peisach D]]
[[Category: Peisach, D.]]
[[Category: Petsko GA]]
[[Category: Petsko, G.A.]]
[[Category: Ringe D]]
[[Category: Ringe, D.]]
[[Category: 8BR]]
[[Category: nucleotide-binding protein]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov  5 14:17:37 2007''

Latest revision as of 14:06, 6 March 2024

HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN (HINT) FROM RABBIT COMPLEXED WITH 8-BR-AMP

5rhn, resolution 2.31Å

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