1ez4
From Proteopedia
(New page: 200px<br /><applet load="1ez4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ez4, resolution 2.3Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1ez4.gif|left|200px]]<br /><applet load="1ez4" size=" | + | [[Image:1ez4.gif|left|200px]]<br /><applet load="1ez4" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ez4, resolution 2.3Å" /> | caption="1ez4, resolution 2.3Å" /> | ||
'''CRYSTAL STRUCTURE OF NON-ALLOSTERIC L-LACTATE DEHYDROGENASE FROM LACTOBACILLUS PENTOSUS AT 2.3 ANGSTROM RESOLUTION'''<br /> | '''CRYSTAL STRUCTURE OF NON-ALLOSTERIC L-LACTATE DEHYDROGENASE FROM LACTOBACILLUS PENTOSUS AT 2.3 ANGSTROM RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | L-Lactate dehydrogenase (LDH) from Lactobacillus pentosus is a | + | L-Lactate dehydrogenase (LDH) from Lactobacillus pentosus is a non-allosteric enzyme, which shows, however, high sequence similarity to allosteric LDHs from certain bacteria. To elucidate the structural basis of the absence of allostery of L. pentosus LDH (LPLDH), we determined the crystal structure of LPLDH at 2.3 A resolution. Bacterial LDHs are tetrameric enzymes composed of identical subunits and exhibit 222 symmetry. The quaternary structure of LPLDH was similar to the active conformation of allosteric LDHs. Structural analysis revealed that the subunit interfaces of LPLDH are optimized mainly through hydrophilic interactions rather than hydrophobic interactions, compared with other LDHs. The subunit interfaces of LPLDH are more specifically stabilized by increased numbers of intersubunit salt bridges and hydrogen bonds, and higher geometrical complementarity. Such high specificity at the subunit interfaces should hinder the rearrangement of the quaternary structure needed for allosteric regulation and thus explain the "non-allostery" of LPLDH. |
==About this Structure== | ==About this Structure== | ||
| - | 1EZ4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lactobacillus_pentosus Lactobacillus pentosus] with NAD as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | + | 1EZ4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lactobacillus_pentosus Lactobacillus pentosus] with <scene name='pdbligand=NAD:'>NAD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1EZ4 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: rossmann fold]] | [[Category: rossmann fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:33:14 2008'' |
Revision as of 10:33, 21 February 2008
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CRYSTAL STRUCTURE OF NON-ALLOSTERIC L-LACTATE DEHYDROGENASE FROM LACTOBACILLUS PENTOSUS AT 2.3 ANGSTROM RESOLUTION
Overview
L-Lactate dehydrogenase (LDH) from Lactobacillus pentosus is a non-allosteric enzyme, which shows, however, high sequence similarity to allosteric LDHs from certain bacteria. To elucidate the structural basis of the absence of allostery of L. pentosus LDH (LPLDH), we determined the crystal structure of LPLDH at 2.3 A resolution. Bacterial LDHs are tetrameric enzymes composed of identical subunits and exhibit 222 symmetry. The quaternary structure of LPLDH was similar to the active conformation of allosteric LDHs. Structural analysis revealed that the subunit interfaces of LPLDH are optimized mainly through hydrophilic interactions rather than hydrophobic interactions, compared with other LDHs. The subunit interfaces of LPLDH are more specifically stabilized by increased numbers of intersubunit salt bridges and hydrogen bonds, and higher geometrical complementarity. Such high specificity at the subunit interfaces should hinder the rearrangement of the quaternary structure needed for allosteric regulation and thus explain the "non-allostery" of LPLDH.
About this Structure
1EZ4 is a Single protein structure of sequence from Lactobacillus pentosus with as ligand. Active as L-lactate dehydrogenase, with EC number 1.1.1.27 Full crystallographic information is available from OCA.
Reference
Crystal structure of non-allosteric L-lactate dehydrogenase from Lactobacillus pentosus at 2.3 A resolution: specific interactions at subunit interfaces., Uchikoba H, Fushinobu S, Wakagi T, Konno M, Taguchi H, Matsuzawa H, Proteins. 2002 Feb 1;46(2):206-14. PMID:11807949
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