This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1je1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1je1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1je1, resolution 1.8&Aring;" /> '''5'-DEOXY-5'-METHYLTHI...)
Current revision (06:03, 3 April 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1je1.jpg|left|200px]]<br /><applet load="1je1" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1je1, resolution 1.8&Aring;" />
 
-
'''5'-DEOXY-5'-METHYLTHIOADENOSINE PHOSPHORYLASE COMPLEX WITH GUANOSINE AND SULFATE'''<br />
 
-
==Overview==
+
==5'-DEOXY-5'-METHYLTHIOADENOSINE PHOSPHORYLASE COMPLEX WITH GUANOSINE AND SULFATE==
-
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.
+
<StructureSection load='1je1' size='340' side='right'caption='[[1je1]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1je1]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JE1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JE1 FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GMP:GUANOSINE'>GMP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1je1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1je1 OCA], [https://pdbe.org/1je1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1je1 RCSB], [https://www.ebi.ac.uk/pdbsum/1je1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1je1 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/PNPH_SACS2 PNPH_SACS2] Cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules. Cleaves inosine, guanosine, and adenosine with a better efficiency than MTA.<ref>PMID:15819883</ref> <ref>PMID:7929153</ref>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/je/1je1_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</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=1je1 ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1JE1 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 GMP 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=1JE1 OCA].
+
*[[5'-deoxy-5'-methylthioadenosine phosphorylase 3D structures|5'-deoxy-5'-methylthioadenosine phosphorylase 3D structures]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11489901 11489901]
+
__TOC__
-
[[Category: S-methyl-5-thioadenosine phosphorylase]]
+
</StructureSection>
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Sulfolobus solfataricus]]
+
[[Category: Saccharolobus solfataricus]]
-
[[Category: Appleby, T.C.]]
+
[[Category: Appleby TC]]
-
[[Category: Cacciapuoti, G.]]
+
[[Category: Cacciapuoti G]]
-
[[Category: Ealick, S.E.]]
+
[[Category: Ealick SE]]
-
[[Category: Mathews, I.I.]]
+
[[Category: Mathews II]]
-
[[Category: Porcelli, M.]]
+
[[Category: Porcelli M]]
-
[[Category: GMP]]
+
-
[[Category: SO4]]
+
-
[[Category: alpha-beta protein]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:09:13 2007''
+

Current revision

5'-DEOXY-5'-METHYLTHIOADENOSINE PHOSPHORYLASE COMPLEX WITH GUANOSINE AND SULFATE

PDB ID 1je1

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1je1"
Personal tools