1f7q: Difference between revisions

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New page: left|200px<br /><applet load="1f7q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f7q, resolution 2.26Å" /> '''CRYSTAL STRUCTURES O...
 
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[[Image:1f7q.gif|left|200px]]<br /><applet load="1f7q" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1f7q.gif|left|200px]]<br /><applet load="1f7q" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1f7q, resolution 2.26&Aring;" />
caption="1f7q, resolution 2.26&Aring;" />
'''CRYSTAL STRUCTURES OF FELINE IMMUNODEFICIENCY VIRUS DUTP PYROPHOSPHATASE AND ITS NUCLEOTIDE COMPLEXES IN THREE CRYSTAL FORMS.'''<br />
'''CRYSTAL STRUCTURES OF FELINE IMMUNODEFICIENCY VIRUS DUTP PYROPHOSPHATASE AND ITS NUCLEOTIDE COMPLEXES IN THREE CRYSTAL FORMS.'''<br />


==Overview==
==Overview==
dUTP pyrophosphatase (dUTPase) cleaves the alpha-beta phosphodiester of, dUTP to form pyrophosphate and dUMP, preventing incorporation of uracil, into DNA and providing the substrate for thymine synthesis. Seven crystal, structures of feline immunodeficiency virus (FIV) dUTPase in three crystal, forms have been determined, including complexes with substrate (dUTP), product (dUMP) or inhibitor (dUDP) bound. The native enzyme has been, refined at 1.40 A resolution in a hexagonal crystal form and at 2.3 A, resolution in an orthorhombic crystal form. In the dUDP complex in a cubic, crystal form refined at 2.5 A resolution, the C-terminal conserved P-loop, motif is fully ordered. The analysis defines the roles of five sequence, motifs in interaction with uracil, deoxyribose and the alpha-, beta- and, gamma-phosphates. The enzyme utilizes adaptive recognition to bind the, alpha- and beta-phosphates. In particular, the alpha-beta phosphodiester, adopts an unfavorable eclipsed conformation in the presence of the P-loop., This conformation may be relevant to the mechanism of alpha-beta, phosphodiester bond cleavage.
dUTP pyrophosphatase (dUTPase) cleaves the alpha-beta phosphodiester of dUTP to form pyrophosphate and dUMP, preventing incorporation of uracil into DNA and providing the substrate for thymine synthesis. Seven crystal structures of feline immunodeficiency virus (FIV) dUTPase in three crystal forms have been determined, including complexes with substrate (dUTP), product (dUMP) or inhibitor (dUDP) bound. The native enzyme has been refined at 1.40 A resolution in a hexagonal crystal form and at 2.3 A resolution in an orthorhombic crystal form. In the dUDP complex in a cubic crystal form refined at 2.5 A resolution, the C-terminal conserved P-loop motif is fully ordered. The analysis defines the roles of five sequence motifs in interaction with uracil, deoxyribose and the alpha-, beta- and gamma-phosphates. The enzyme utilizes adaptive recognition to bind the alpha- and beta-phosphates. In particular, the alpha-beta phosphodiester adopts an unfavorable eclipsed conformation in the presence of the P-loop. This conformation may be relevant to the mechanism of alpha-beta phosphodiester bond cleavage.


==About this Structure==
==About this Structure==
1F7Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Feline_immunodeficiency_virus Feline immunodeficiency virus] with DUT as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/dUTP_diphosphatase dUTP diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.23 3.6.1.23] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F7Q OCA].  
1F7Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Feline_immunodeficiency_virus Feline immunodeficiency virus] with <scene name='pdbligand=DUT:'>DUT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/dUTP_diphosphatase dUTP diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.23 3.6.1.23] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F7Q OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: dUTP diphosphatase]]
[[Category: dUTP diphosphatase]]
[[Category: Elder, J.H.]]
[[Category: Elder, J H.]]
[[Category: Prasad, G.S.]]
[[Category: Prasad, G S.]]
[[Category: Stout, C.D.]]
[[Category: Stout, C D.]]
[[Category: Stura, E.A.]]
[[Category: Stura, E A.]]
[[Category: DUT]]
[[Category: DUT]]
[[Category: eight stranded beta barrel protein]]
[[Category: eight stranded beta barrel protein]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:40:59 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:35:44 2008''

Revision as of 13:35, 21 February 2008

File:1f7q.gif


1f7q, resolution 2.26Å

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CRYSTAL STRUCTURES OF FELINE IMMUNODEFICIENCY VIRUS DUTP PYROPHOSPHATASE AND ITS NUCLEOTIDE COMPLEXES IN THREE CRYSTAL FORMS.

OverviewOverview

dUTP pyrophosphatase (dUTPase) cleaves the alpha-beta phosphodiester of dUTP to form pyrophosphate and dUMP, preventing incorporation of uracil into DNA and providing the substrate for thymine synthesis. Seven crystal structures of feline immunodeficiency virus (FIV) dUTPase in three crystal forms have been determined, including complexes with substrate (dUTP), product (dUMP) or inhibitor (dUDP) bound. The native enzyme has been refined at 1.40 A resolution in a hexagonal crystal form and at 2.3 A resolution in an orthorhombic crystal form. In the dUDP complex in a cubic crystal form refined at 2.5 A resolution, the C-terminal conserved P-loop motif is fully ordered. The analysis defines the roles of five sequence motifs in interaction with uracil, deoxyribose and the alpha-, beta- and gamma-phosphates. The enzyme utilizes adaptive recognition to bind the alpha- and beta-phosphates. In particular, the alpha-beta phosphodiester adopts an unfavorable eclipsed conformation in the presence of the P-loop. This conformation may be relevant to the mechanism of alpha-beta phosphodiester bond cleavage.

About this StructureAbout this Structure

1F7Q is a Single protein structure of sequence from Feline immunodeficiency virus with as ligand. Active as dUTP diphosphatase, with EC number 3.6.1.23 Full crystallographic information is available from OCA.

ReferenceReference

Structures of feline immunodeficiency virus dUTP pyrophosphatase and its nucleotide complexes in three crystal forms., Prasad GS, Stura EA, Elder JH, Stout CD, Acta Crystallogr D Biol Crystallogr. 2000 Sep;56(Pt 9):1100-9. PMID:10957629

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