1f3y
From Proteopedia
(New page: 200px<br /><applet load="1f3y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f3y" /> '''SOLUTION STRUCTURE OF THE NUDIX ENZYME DIADE...) |
|||
Line 1: | Line 1: | ||
- | [[Image:1f3y.jpg|left|200px]]<br /><applet load="1f3y" size=" | + | [[Image:1f3y.jpg|left|200px]]<br /><applet load="1f3y" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1f3y" /> | caption="1f3y" /> | ||
'''SOLUTION STRUCTURE OF THE NUDIX ENZYME DIADENOSINE TETRAPHOSPHATE HYDROLASE FROM LUPINUS ANGUSTIFOLIUS L.'''<br /> | '''SOLUTION STRUCTURE OF THE NUDIX ENZYME DIADENOSINE TETRAPHOSPHATE HYDROLASE FROM LUPINUS ANGUSTIFOLIUS L.'''<br /> | ||
==Overview== | ==Overview== | ||
- | The solution structure of diadenosine 5',5'''-P1,P4-tetraphosphate | + | The solution structure of diadenosine 5',5'''-P1,P4-tetraphosphate hydrolase from Lupinus angustifolius L., an enzyme of the Nudix family, has been determined by heteronuclear NMR, using a torsion angle dynamics/simulated annealing protocol based on approximately 12 interresidue NOEs per residue. The structure represents the first Ap4A hydrolase to be determined, and sequence homology suggests that other members will have the same fold. The family of structures shows a well-defined fold comprised of a central four-stranded mixed beta-sheet, a two-stranded antiparallel beta-sheet and three helices (alphaI, alphaIII, alphaIV). The root-mean-squared deviation for the backbone (C',O,N,Calpha) of the rigid parts (residues 9 to 75, 97 to 115, 125 to 160) of the protein is 0.32 A. Several regions, however, show lower definition, particularly an isolated helix (alphaII) that connects two strands of the central sheet. This poor definition is mainly due to a lack of long-range NOEs between alphaII and other parts of the protein. Mapping conserved residues outside of the Nudix signature and those sensitive to an Ap4A analogue suggests that the adenosine-ribose moiety of the substrate binds into a large cleft above the four-stranded beta-sheet. Four conserved glutamate residues (Glu55, Glu58, Glu59 and Glu125) form a cluster that most likely ligates an essential magnesium ion, however, Gly41 also an expected magnesium ligand, is distant from this cluster. |
==About this Structure== | ==About this Structure== | ||
- | 1F3Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lupinus_angustifolius Lupinus angustifolius]. Active as [http://en.wikipedia.org/wiki/Bis(5'-nucleosyl)-tetraphosphatase_(asymmetrical) Bis(5'-nucleosyl)-tetraphosphatase (asymmetrical)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.17 3.6.1.17] Full crystallographic information is available from [http:// | + | 1F3Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lupinus_angustifolius Lupinus angustifolius]. Active as [http://en.wikipedia.org/wiki/Bis(5'-nucleosyl)-tetraphosphatase_(asymmetrical) Bis(5'-nucleosyl)-tetraphosphatase (asymmetrical)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.17 3.6.1.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F3Y OCA]. |
==Reference== | ==Reference== | ||
Line 15: | Line 15: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bashtannyk, T.]] | [[Category: Bashtannyk, T.]] | ||
- | [[Category: Blackburn, G | + | [[Category: Blackburn, G M.]] |
- | [[Category: Gayler, K | + | [[Category: Gayler, K R.]] |
- | [[Category: Gooley, P | + | [[Category: Gooley, P R.]] |
[[Category: Maksel, D.]] | [[Category: Maksel, D.]] | ||
- | [[Category: Swarbrick, J | + | [[Category: Swarbrick, J D.]] |
- | [[Category: Zhang, X | + | [[Category: Zhang, X R.]] |
[[Category: 2-stranded antiparallel sheet]] | [[Category: 2-stranded antiparallel sheet]] | ||
[[Category: alpha-beta-alpha sandwich]] | [[Category: alpha-beta-alpha sandwich]] | ||
Line 26: | Line 26: | ||
[[Category: mixed 4-stranded beta sheet]] | [[Category: mixed 4-stranded beta sheet]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:34:36 2008'' |
Revision as of 10:34, 21 February 2008
|
SOLUTION STRUCTURE OF THE NUDIX ENZYME DIADENOSINE TETRAPHOSPHATE HYDROLASE FROM LUPINUS ANGUSTIFOLIUS L.
Overview
The solution structure of diadenosine 5',5-P1,P4-tetraphosphate hydrolase from Lupinus angustifolius L., an enzyme of the Nudix family, has been determined by heteronuclear NMR, using a torsion angle dynamics/simulated annealing protocol based on approximately 12 interresidue NOEs per residue. The structure represents the first Ap4A hydrolase to be determined, and sequence homology suggests that other members will have the same fold. The family of structures shows a well-defined fold comprised of a central four-stranded mixed beta-sheet, a two-stranded antiparallel beta-sheet and three helices (alphaI, alphaIII, alphaIV). The root-mean-squared deviation for the backbone (C',O,N,Calpha) of the rigid parts (residues 9 to 75, 97 to 115, 125 to 160) of the protein is 0.32 A. Several regions, however, show lower definition, particularly an isolated helix (alphaII) that connects two strands of the central sheet. This poor definition is mainly due to a lack of long-range NOEs between alphaII and other parts of the protein. Mapping conserved residues outside of the Nudix signature and those sensitive to an Ap4A analogue suggests that the adenosine-ribose moiety of the substrate binds into a large cleft above the four-stranded beta-sheet. Four conserved glutamate residues (Glu55, Glu58, Glu59 and Glu125) form a cluster that most likely ligates an essential magnesium ion, however, Gly41 also an expected magnesium ligand, is distant from this cluster.
About this Structure
1F3Y is a Single protein structure of sequence from Lupinus angustifolius. Active as Bis(5'-nucleosyl)-tetraphosphatase (asymmetrical), with EC number 3.6.1.17 Full crystallographic information is available from OCA.
Reference
The three-dimensional structure of the Nudix enzyme diadenosine tetraphosphate hydrolase from Lupinus angustifolius L., Swarbrick JD, Bashtannyk T, Maksel D, Zhang XR, Blackburn GM, Gayler KR, Gooley PR, J Mol Biol. 2000 Oct 6;302(5):1165-77. PMID:11183782
Page seeded by OCA on Thu Feb 21 12:34:36 2008
Categories: Bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) | Lupinus angustifolius | Single protein | Bashtannyk, T. | Blackburn, G M. | Gayler, K R. | Gooley, P R. | Maksel, D. | Swarbrick, J D. | Zhang, X R. | 2-stranded antiparallel sheet | Alpha-beta-alpha sandwich | Enzyme | Mixed 4-stranded beta sheet