3fit: Difference between revisions
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[[Image:3fit.gif|left|200px]] | [[Image:3fit.gif|left|200px]] | ||
'''FHIT (FRAGILE HISTIDINE TRIAD PROTEIN) IN COMPLEX WITH ADENOSINE/SULFATE AMP ANALOG''' | {{Structure | ||
|PDB= 3fit |SIZE=350|CAPTION= <scene name='initialview01'>3fit</scene>, resolution 2.4Å | |||
|SITE= <scene name='pdbsite=AVE:Catalytic+HIS'>AVE</scene> | |||
|LIGAND= <scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=A:ADENOSINE-5'-MONOPHOSPHATE'>A</scene> | |||
|ACTIVITY= | |||
|GENE= FHIT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''FHIT (FRAGILE HISTIDINE TRIAD PROTEIN) IN COMPLEX WITH ADENOSINE/SULFATE AMP ANALOG''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
3FIT is a [ | 3FIT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FIT OCA]. | ||
==Reference== | ==Reference== | ||
MAD analysis of FHIT, a putative human tumor suppressor from the HIT protein family., Lima CD, D'Amico KL, Naday I, Rosenbaum G, Westbrook EM, Hendrickson WA, Structure. 1997 Jun 15;5(6):763-74. PMID:[http:// | MAD analysis of FHIT, a putative human tumor suppressor from the HIT protein family., Lima CD, D'Amico KL, Naday I, Rosenbaum G, Westbrook EM, Hendrickson WA, Structure. 1997 Jun 15;5(6):763-74. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9261067 9261067] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: advanced photon source]] | [[Category: advanced photon source]] | ||
[[Category: | [[Category: ap]] | ||
[[Category: complex (chromosomal translocation/ade)]] | [[Category: complex (chromosomal translocation/ade)]] | ||
[[Category: fhit]] | [[Category: fhit]] | ||
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[[Category: putative human tumor suppressor]] | [[Category: putative human tumor suppressor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:04:48 2008'' | ||
Revision as of 20:04, 20 March 2008
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| , resolution 2.4Å | |||||||
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| Sites: | |||||||
| Ligands: | , and | ||||||
| Gene: | FHIT (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
FHIT (FRAGILE HISTIDINE TRIAD PROTEIN) IN COMPLEX WITH ADENOSINE/SULFATE AMP ANALOG
OverviewOverview
BACKGROUND: The fragile histidine triad (FHIT) protein is a member of the large and ubiquitous histidine triad (HIT) family of proteins. It is expressed from a gene located at a fragile site on human chromosome 3, which is commonly disrupted in association with certain cancers. On the basis of the genetic evidence, it has been postulated that the FHIT protein may function as a tumor suppressor, implying a role for the FHIT protein in carcinogenesis. The FHIT protein has dinucleoside polyphosphate hydrolase activity in vitro, thus suggesting that its role in vivo may involve the hydrolysis of a phosphoanhydride bond. The structural analysis of FHIT will identify critical residues involved in substrate binding and catalysis, and will provide insights into the in vivo function of HIT proteins. RESULTS: The three-dimensional crystal structures of free and nucleoside complexed FHIT have been determined from multiwavelength anomalous diffraction (MAD) data, and they represent some of the first successful structures to be measured with undulator radiation at the Advanced Photon Source. The structures of FHIT reveal that this protein exists as an intimate homodimer, which is based on a core structure observed previously in another human HIT homolog, protein kinase C interacting protein (PKCI), but has distinctive elaborations at both the N and C termini. Conserved residues within the HIT family, which are involved in the interactions of the proteins with nucleoside and phosphate groups, appear to be relevant for the catalytic activity of this protein. CONCLUSIONS: The structure of FHIT, a divergent HIT protein family member, in complex with a nucleotide analog suggests a metal-independent catalytic mechanism for the HIT family of proteins. A structural comparison of FHIT with PKCI and galactose-1-phosphate uridylyltransferase (GaIT) reveals additional implications for the structural and functional evolution of the ubiquitous HIT family of proteins.
About this StructureAbout this Structure
3FIT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
MAD analysis of FHIT, a putative human tumor suppressor from the HIT protein family., Lima CD, D'Amico KL, Naday I, Rosenbaum G, Westbrook EM, Hendrickson WA, Structure. 1997 Jun 15;5(6):763-74. PMID:9261067
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