1lon: Difference between revisions
New page: left|200px<br /><applet load="1lon" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lon, resolution 2.1Å" /> '''Crystal Structure of ... |
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[[Image:1lon.gif|left|200px]]<br /><applet load="1lon" size=" | [[Image:1lon.gif|left|200px]]<br /><applet load="1lon" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1lon, resolution 2.1Å" /> | caption="1lon, resolution 2.1Å" /> | ||
'''Crystal Structure of the Recombinant Mouse-Muscle Adenylosuccinate Synthetase Complexed with 6-phosphoryl-IMP, GDP and Hadacidin'''<br /> | '''Crystal Structure of the Recombinant Mouse-Muscle Adenylosuccinate Synthetase Complexed with 6-phosphoryl-IMP, GDP and Hadacidin'''<br /> | ||
==Overview== | ==Overview== | ||
Prokaryotes have a single form of adenylosuccinate synthetase that | Prokaryotes have a single form of adenylosuccinate synthetase that controls the committed step of AMP biosynthesis, but vertebrates have two isozymes of the synthetase. The basic isozyme, which predominates in muscle, participates in the purine nucleotide cycle, has an active site conformation different from that of the Escherichia coli enzyme, and exhibits significant differences in ligand recognition. Crystalline complexes presented here of the recombinant basic isozyme from mouse show the following. GTP alone binds to the active site without inducing a conformational change. IMP in combination with an acetate anion induces major conformational changes and organizes the active site for catalysis. IMP, in the absence of GTP, binds to the GTP pocket of the synthetase. The combination of GTP and IMP results in the formation of a stable complex of 6-phosphoryl-IMP and GDP in the presence or absence of hadacidin. The response of the basic isozyme to GTP alone differs from that of synthetases from plants, and yet the conformation of the mouse basic and E. coli synthetases in their complexes with GDP, 6-phosphoryl-IMP, and hadacidin are nearly identical. Hence, reported differences in ligand recognition among synthetases probably arise from conformational variations observed in partially ligated enzymes. | ||
==About this Structure== | ==About this Structure== | ||
1LON is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with MG, IMO, HDA and GDP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Adenylosuccinate_synthase Adenylosuccinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.4 6.3.4.4] Full crystallographic information is available from [http:// | 1LON is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=IMO:'>IMO</scene>, <scene name='pdbligand=HDA:'>HDA</scene> and <scene name='pdbligand=GDP:'>GDP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Adenylosuccinate_synthase Adenylosuccinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.4 6.3.4.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LON OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Borza, T.]] | [[Category: Borza, T.]] | ||
[[Category: Fromm, H | [[Category: Fromm, H J.]] | ||
[[Category: Honzatko, R | [[Category: Honzatko, R B.]] | ||
[[Category: Iancu, C | [[Category: Iancu, C V.]] | ||
[[Category: GDP]] | [[Category: GDP]] | ||
[[Category: HDA]] | [[Category: HDA]] | ||
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[[Category: purine biosynthesis]] | [[Category: purine biosynthesis]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:46:53 2008'' |