1hyh
From Proteopedia
(New page: 200px<br /><applet load="1hyh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hyh, resolution 2.2Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1hyh.jpg|left|200px]]<br /><applet load="1hyh" size=" | + | [[Image:1hyh.jpg|left|200px]]<br /><applet load="1hyh" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1hyh, resolution 2.2Å" /> | caption="1hyh, resolution 2.2Å" /> | ||
'''CRYSTAL STRUCTURE OF L-2-HYDROXYISOCAPROATE DEHYDROGENASE FROM LACTOBACILLUS CONFUSUS AT 2.2 ANGSTROMS RESOLUTION-AN EXAMPLE OF STRONG ASYMMETRY BETWEEN SUBUNITS'''<br /> | '''CRYSTAL STRUCTURE OF L-2-HYDROXYISOCAPROATE DEHYDROGENASE FROM LACTOBACILLUS CONFUSUS AT 2.2 ANGSTROMS RESOLUTION-AN EXAMPLE OF STRONG ASYMMETRY BETWEEN SUBUNITS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | L-2-Hydroxyisocaproate dehydrogenase (L-HicDH) from Lactobacillus | + | L-2-Hydroxyisocaproate dehydrogenase (L-HicDH) from Lactobacillus confusus, a homotetramer with a molecular mass of 33 kDa per subunit, belongs to the protein family of the NAD(+)-dependent L-2-hydroxycarboxylate dehydrogenases. L-HicDH was crystallized with ammonium sulphate as precipitant in the presence of NAD+. The crystals belong to the trigonal space group P3(2)21, with a = 135.9 A and c = 205.9 A, and diffract X-rays to 2.2 A resolution. The crystal structure was solved by Patterson search and molecular replacement techniques and refined to an R-value of 21.4% (2.2 to 8 A). The final structure model contains one NAD+ molecule and one sulphate ion per subunit, with 309 water molecules. An unusual feature of this crystal structure is the deviation of the protein subunits from non-crystallographic symmetry, which is so strong that it can be detected globally by self-rotation calculations in reciprocal space. This asymmetry is especially pronounced in the environment of the active site; it is reflected also in the nicotinamide conformation of NAD+ and allows some conclusions to be drawn about the catalytic mechanism. In this context, an "inner active site loop" is identified as a structural element of fundamental functional importance. Furthermore, with knowledge of the crystal structure of L-HicDH the differences in substrate specificity between L-HicDH and the L-lactate dehydrogenases can be partly explained. |
==About this Structure== | ==About this Structure== | ||
| - | 1HYH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Weissella_confusa Weissella confusa] with SO4 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:// | + | 1HYH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Weissella_confusa Weissella confusa] with <scene name='pdbligand=SO4:'>SO4</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=1HYH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Weissella confusa]] | [[Category: Weissella confusa]] | ||
| - | [[Category: Hecht, H | + | [[Category: Hecht, H J.]] |
[[Category: Niefind, K.]] | [[Category: Niefind, K.]] | ||
[[Category: Schomburg, D.]] | [[Category: Schomburg, D.]] | ||
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[[Category: l-lactate dehydrogenase]] | [[Category: l-lactate dehydrogenase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:06:11 2008'' |
Revision as of 11:06, 21 February 2008
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CRYSTAL STRUCTURE OF L-2-HYDROXYISOCAPROATE DEHYDROGENASE FROM LACTOBACILLUS CONFUSUS AT 2.2 ANGSTROMS RESOLUTION-AN EXAMPLE OF STRONG ASYMMETRY BETWEEN SUBUNITS
Overview
L-2-Hydroxyisocaproate dehydrogenase (L-HicDH) from Lactobacillus confusus, a homotetramer with a molecular mass of 33 kDa per subunit, belongs to the protein family of the NAD(+)-dependent L-2-hydroxycarboxylate dehydrogenases. L-HicDH was crystallized with ammonium sulphate as precipitant in the presence of NAD+. The crystals belong to the trigonal space group P3(2)21, with a = 135.9 A and c = 205.9 A, and diffract X-rays to 2.2 A resolution. The crystal structure was solved by Patterson search and molecular replacement techniques and refined to an R-value of 21.4% (2.2 to 8 A). The final structure model contains one NAD+ molecule and one sulphate ion per subunit, with 309 water molecules. An unusual feature of this crystal structure is the deviation of the protein subunits from non-crystallographic symmetry, which is so strong that it can be detected globally by self-rotation calculations in reciprocal space. This asymmetry is especially pronounced in the environment of the active site; it is reflected also in the nicotinamide conformation of NAD+ and allows some conclusions to be drawn about the catalytic mechanism. In this context, an "inner active site loop" is identified as a structural element of fundamental functional importance. Furthermore, with knowledge of the crystal structure of L-HicDH the differences in substrate specificity between L-HicDH and the L-lactate dehydrogenases can be partly explained.
About this Structure
1HYH is a Single protein structure of sequence from Weissella confusa with and as ligands. Active as L-lactate dehydrogenase, with EC number 1.1.1.27 Full crystallographic information is available from OCA.
Reference
Crystal structure of L-2-hydroxyisocaproate dehydrogenase from Lactobacillus confusus at 2.2 A resolution. An example of strong asymmetry between subunits., Niefind K, Hecht HJ, Schomburg D, J Mol Biol. 1995 Aug 11;251(2):256-81. PMID:7643402
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