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6fit

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[[Image:6fit.jpg|left|200px]]<br /><applet load="6fit" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="6fit, resolution 2.6&Aring;" />
 
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'''FHIT-TRANSITION STATE ANALOG'''<br />
 
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==Overview==
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==FHIT-TRANSITION STATE ANALOG==
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The histidine triad (HIT) protein family is among the most ubiquitous and highly conserved in nature, but a biological activity has not yet been identified for any member of the HIT family. Fragile histidine triad protein (FHIT) and protein kinase C interacting protein (PKCI) were used in a structure-based approach to elucidate characteristics of in vivo ligands and reactions. Crystallographic structures of apo, substrate analog, pentacovalent transition-state analog, and product states of both enzymes reveal a catalytic mechanism and define substrate characteristics required for catalysis, thus unifying the HIT family as nucleotidyl hydrolases, transferases, or both. The approach described here may be useful in identifying structure-function relations between protein families identified through genomics.
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<StructureSection load='6fit' size='340' side='right'caption='[[6fit]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6fit]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FIT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FIT FirstGlance]. <br>
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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]] 2.6&#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=AMW:ADENOSINE+MONOTUNGSTATE'>AMW</scene></td></tr>
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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=6fit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fit OCA], [https://pdbe.org/6fit PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fit RCSB], [https://www.ebi.ac.uk/pdbsum/6fit PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fit ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/FHIT_HUMAN FHIT_HUMAN] Note=A chromosomal aberration involving FHIT has been found in a lymphoblastoid cell line established from a family with renal cell carcinoma and thyroid carcinoma. Translocation t(3;8)(p14.2;q24.1) with RNF139. Although the 3p14.2 breakpoint has been shown to interrupt FHIT in its 5-prime non-coding region, it is unlikely that FHIT is causally related to renal or other malignancies.<ref>PMID:15007172</ref> Note=Associated with digestive tract cancers. Numerous tumor types are found to have aberrant forms of FHIT protein due to deletions in a coding region of chromosome 3p14.2 including the fragile site locus FRA3B.<ref>PMID:15007172</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/FHIT_HUMAN FHIT_HUMAN] Cleaves A-5'-PPP-5'A to yield AMP and ADP. Possible tumor suppressor for specific tissues.<ref>PMID:8794732</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/fi/6fit_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=6fit ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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6FIT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=AMW:'>AMW</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Bis(5'-adenosyl)-triphosphatase Bis(5'-adenosyl)-triphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.29 3.6.1.29] Known structural/functional Sites: <scene name='pdbsite=AVE:Active+Site+HIS+Responsible+For+Forming+The+Transient+Nu+...'>AVE</scene> and <scene name='pdbsite=HNE:HIS+Triad+For+Which+This+Family+Was+Named'>HNE</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FIT OCA].
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*[[Histidine triad nucleotide-binding protein 3D structures|Histidine triad nucleotide-binding protein 3D structures]]
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== References ==
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==Reference==
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<references/>
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Structure-based analysis of catalysis and substrate definition in the HIT protein family., Lima CD, Klein MG, Hendrickson WA, Science. 1997 Oct 10;278(5336):286-90. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9323207 9323207]
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__TOC__
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[[Category: Bis(5'-adenosyl)-triphosphatase]]
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Hendrickson, W A.]]
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[[Category: Hendrickson WA]]
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[[Category: Klein, M G.]]
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[[Category: Klein MG]]
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[[Category: Lima, C D.]]
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[[Category: Lima CD]]
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[[Category: AMW]]
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[[Category: fhit]]
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[[Category: fragile histidine triad protein]]
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[[Category: histidine triad protein family]]
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[[Category: hit protein family]]
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[[Category: hydrolase]]
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[[Category: nucleotidyl hydrolase]]
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[[Category: nucleotidyl transferase]]
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[[Category: putative tumor suppressor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:16:33 2008''
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Current revision

FHIT-TRANSITION STATE ANALOG

PDB ID 6fit

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