1jdv: Difference between revisions

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CRYSTAL STRUCTURE OF 5'-DEOXY-5'-METHYLTHIOADENOSINE PHOSPHORYLASE COMPLEXED WITH ADENOSINE AND SULFATE ION

OverviewOverview

The structure of 5'-deoxy-5'-methylthioadenosine phosphorylase from Sulfolobus solfataricus (SsMTAP) has been determined alone, as ternary complexes with sulfate plus substrates 5'-deoxy-5'-methylthioadenosine, adenosine, or guanosine, or with the noncleavable substrate analog Formycin B and as binary complexes with phosphate or sulfate alone. The structure of unliganded SsMTAP was refined at 2.5-A resolution and the structures of the complexes were refined at resolutions ranging from 1.6 to 2.0 A. SsMTAP is unusual both for its broad substrate specificity and for its extreme thermal stability. The hexameric structure of SsMTAP is similar to that of purine-nucleoside phosphorylase (PNP) from Escherichia coli, however, only SsMTAP accepts 5'-deoxy-5'-methylthioadenosine as a substrate. The active site of SsMTAP is similar to that of E. coli PNP with 13 of 18 nearest residues being identical. The main differences are at Thr(89), which corresponds to serine in E. coli PNP, and Glu(163), which corresponds to proline in E. coli PNP. In addition, a water molecule is found near the purine N-7 position in the guanosine complex of SsMTAP. Thr(89) is near the 5'-position of the nucleoside and may account for the ability of SsMTAP to accept either hydrophobic or hydrophilic substituents in that position. Unlike E. coli PNP, the structures of SsMTAP reveal a substrate-induced conformational change involving Glu(163). This residue is located at the interface between subunits and swings in toward the active site upon nucleoside binding. The high-resolution structures of SsMTAP suggest that the transition state is stabilized in different ways for 6-amino versus 6-oxo substrates. SsMTAP has optimal activity at 120 degrees C and retains full activity after 2 h at 100 degrees C. Examination of the three-dimensional structure of SsMTAP suggests that unlike most thermophilic enzymes, disulfide linkages play a key in role in its thermal stability.

About this StructureAbout this Structure

1JDV is a Single protein structure of sequence from Sulfolobus solfataricus with and as ligands. Active as S-methyl-5-thioadenosine phosphorylase, with EC number 2.4.2.28 Full crystallographic information is available from OCA.

ReferenceReference

Three-dimensional structure of a hyperthermophilic 5'-deoxy-5'-methylthioadenosine phosphorylase from Sulfolobus solfataricus., Appleby TC, Mathews II, Porcelli M, Cacciapuoti G, Ealick SE, J Biol Chem. 2001 Oct 19;276(42):39232-42. Epub 2001 Aug 6. PMID:11489901

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-[[Image:1jdv.jpg|left|200px]]<br /><applet load="1jdv" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1jdv.jpg|left|200px]]<br /><applet load="1jdv" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1jdv, resolution 2.0&Aring;" />
 '''CRYSTAL STRUCTURE OF 5'-DEOXY-5'-METHYLTHIOADENOSINE PHOSPHORYLASE COMPLEXED WITH ADENOSINE AND SULFATE ION'''<br />
 ==Overview==
-The structure of 5'-deoxy-5'-methylthioadenosine phosphorylase from, Sulfolobus solfataricus (SsMTAP) has been determined alone, as ternary, complexes with sulfate plus substrates 5'-deoxy-5'-methylthioadenosine, adenosine, or guanosine, or with the noncleavable substrate analog, Formycin B and as binary complexes with phosphate or sulfate alone. The, structure of unliganded SsMTAP was refined at 2.5-A resolution and the, structures of the complexes were refined at resolutions ranging from 1.6, to 2.0 A. SsMTAP is unusual both for its broad substrate specificity and, for its extreme thermal stability. The hexameric structure of SsMTAP is, similar to that of purine-nucleoside phosphorylase (PNP) from Escherichia, coli, however, only SsMTAP accepts 5'-deoxy-5'-methylthioadenosine as a, substrate. The active site of SsMTAP is similar to that of E. coli PNP, with 13 of 18 nearest residues being identical. The main differences are, at Thr(89), which corresponds to serine in E. coli PNP, and Glu(163), which corresponds to proline in E. coli PNP. In addition, a water molecule, is found near the purine N-7 position in the guanosine complex of SsMTAP., Thr(89) is near the 5'-position of the nucleoside and may account for the, ability of SsMTAP to accept either hydrophobic or hydrophilic substituents, in that position. Unlike E. coli PNP, the structures of SsMTAP reveal a, substrate-induced conformational change involving Glu(163). This residue, is located at the interface between subunits and swings in toward the, active site upon nucleoside binding. The high-resolution structures of, SsMTAP suggest that the transition state is stabilized in different ways, for 6-amino versus 6-oxo substrates. SsMTAP has optimal activity at 120, degrees C and retains full activity after 2 h at 100 degrees C., Examination of the three-dimensional structure of SsMTAP suggests that, unlike most thermophilic enzymes, disulfide linkages play a key in role in, its thermal stability.
+The structure of 5'-deoxy-5'-methylthioadenosine phosphorylase from Sulfolobus solfataricus (SsMTAP) has been determined alone, as ternary complexes with sulfate plus substrates 5'-deoxy-5'-methylthioadenosine, adenosine, or guanosine, or with the noncleavable substrate analog Formycin B and as binary complexes with phosphate or sulfate alone. The structure of unliganded SsMTAP was refined at 2.5-A resolution and the structures of the complexes were refined at resolutions ranging from 1.6 to 2.0 A. SsMTAP is unusual both for its broad substrate specificity and for its extreme thermal stability. The hexameric structure of SsMTAP is similar to that of purine-nucleoside phosphorylase (PNP) from Escherichia coli, however, only SsMTAP accepts 5'-deoxy-5'-methylthioadenosine as a substrate. The active site of SsMTAP is similar to that of E. coli PNP with 13 of 18 nearest residues being identical. The main differences are at Thr(89), which corresponds to serine in E. coli PNP, and Glu(163), which corresponds to proline in E. coli PNP. In addition, a water molecule is found near the purine N-7 position in the guanosine complex of SsMTAP. Thr(89) is near the 5'-position of the nucleoside and may account for the ability of SsMTAP to accept either hydrophobic or hydrophilic substituents in that position. Unlike E. coli PNP, the structures of SsMTAP reveal a substrate-induced conformational change involving Glu(163). This residue is located at the interface between subunits and swings in toward the active site upon nucleoside binding. The high-resolution structures of SsMTAP suggest that the transition state is stabilized in different ways for 6-amino versus 6-oxo substrates. SsMTAP has optimal activity at 120 degrees C and retains full activity after 2 h at 100 degrees C. Examination of the three-dimensional structure of SsMTAP suggests that unlike most thermophilic enzymes, disulfide linkages play a key in role in its thermal stability.
 ==About this Structure==
-JDV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus] with SO4 and ADN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/S-methyl-5-thioadenosine_phosphorylase S-methyl-5-thioadenosine phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.28 2.4.2.28] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JDV OCA].
+JDV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=ADN:'>ADN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/S-methyl-5-thioadenosine_phosphorylase S-methyl-5-thioadenosine phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.28 2.4.2.28] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JDV OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Sulfolobus solfataricus]]
-[[Category: Appleby, T.C.]]
+[[Category: Appleby, T C.]]
 [[Category: Cacciapuoti, G.]]
-[[Category: Ealick, S.E.]]
+[[Category: Ealick, S E.]]
-[[Category: Mathews, I.I.]]
+[[Category: Mathews, I I.]]
 [[Category: Porcelli, M.]]
 [[Category: ADN]]
@@ Line 23: / Line 23: @@
 [[Category: alpha-beta protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:08:58 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:21:33 2008''