1ldn: Difference between revisions
New page: left|200px<br /><applet load="1ldn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ldn, resolution 2.5Å" /> '''STRUCTURE OF A TERNAR... |
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[[Image:1ldn.gif|left|200px]]<br /><applet load="1ldn" size=" | [[Image:1ldn.gif|left|200px]]<br /><applet load="1ldn" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ldn, resolution 2.5Å" /> | caption="1ldn, resolution 2.5Å" /> | ||
'''STRUCTURE OF A TERNARY COMPLEX OF AN ALLOSTERIC LACTATE DEHYDROGENASE FROM BACILLUS STEAROTHERMOPHILUS AT 2.5 ANGSTROMS RESOLUTION'''<br /> | '''STRUCTURE OF A TERNARY COMPLEX OF AN ALLOSTERIC LACTATE DEHYDROGENASE FROM BACILLUS STEAROTHERMOPHILUS AT 2.5 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
We report the refined structure of a ternary complex of an allosterically | We report the refined structure of a ternary complex of an allosterically activated lactate dehydrogenase, including the important active site loop. Eightfold non-crystallographic symmetry averaging was utilized to improve the density maps. Interactions between the protein and bound coenzyme and oxamate are described in relation to other studies using site-specific mutagenesis. Fructose 1,6-bisphosphate (FruP2) is bound to the enzyme across one of the 2-fold axes of the tetramer, with the two phosphate moieties interacting with two anion binding sites, one on each of two subunits, across this interface. However, because FruP2 binds at this special site, yet does not possess an internal 2-fold symmetry axis, the ligand is statistically disordered and binds to each site in two different orientations. Binding of FruP2 to the tetramer is signalled to the active site principally through two interactions with His188 and Arg173. His188 is connected to His195 (which binds the carbonyl group of the substrate) and Arg173 is connected to Arg171 (the residue that binds the carboxylate group of the substrate). | ||
==About this Structure== | ==About this Structure== | ||
1LDN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with FBP, OXM and NAD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/L-lactate_dehydrogenase L-lactate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.27 1.1.1.27] Full crystallographic information is available from [http:// | 1LDN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with <scene name='pdbligand=FBP:'>FBP</scene>, <scene name='pdbligand=OXM:'>OXM</scene> and <scene name='pdbligand=NAD:'>NAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/L-lactate_dehydrogenase L-lactate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.27 1.1.1.27] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LDN OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: L-lactate dehydrogenase]] | [[Category: L-lactate dehydrogenase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Dodson, E | [[Category: Dodson, E J.]] | ||
[[Category: Gamblin, S | [[Category: Gamblin, S J.]] | ||
[[Category: Holbrook, J | [[Category: Holbrook, J J.]] | ||
[[Category: Muirhead, H.]] | [[Category: Muirhead, H.]] | ||
[[Category: Piontek, K.]] | [[Category: Piontek, K.]] | ||
[[Category: Turkenburg, J | [[Category: Turkenburg, J P.]] | ||
[[Category: Wigley, D | [[Category: Wigley, D B.]] | ||
[[Category: FBP]] | [[Category: FBP]] | ||
[[Category: NAD]] | [[Category: NAD]] | ||
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[[Category: oxidoreductase(choh(d)-nad(a))]] | [[Category: oxidoreductase(choh(d)-nad(a))]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:44:00 2008'' | ||
