1guy: Difference between revisions
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[[Image:1guy.gif|left|200px]] | [[Image:1guy.gif|left|200px]] | ||
'''STRUCTURAL BASIS FOR THERMOPHILIC PROTEIN STABILITY: STRUCTURES OF THERMOPHILIC AND MESOPHILIC MALATE DEHYDROGENASES''' | {{Structure | ||
|PDB= 1guy |SIZE=350|CAPTION= <scene name='initialview01'>1guy</scene>, resolution 2.20Å | |||
|SITE= <scene name='pdbsite=AC1:Cd+Binding+Site+For+Chain+C'>AC1</scene> | |||
|LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene> and <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Malate_dehydrogenase Malate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.37 1.1.1.37] | |||
|GENE= | |||
}} | |||
'''STRUCTURAL BASIS FOR THERMOPHILIC PROTEIN STABILITY: STRUCTURES OF THERMOPHILIC AND MESOPHILIC MALATE DEHYDROGENASES''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1GUY is a [ | 1GUY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Chloroflexus_aurantiacus Chloroflexus aurantiacus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GUY OCA]. | ||
==Reference== | ==Reference== | ||
Structural basis for thermophilic protein stability: structures of thermophilic and mesophilic malate dehydrogenases., Dalhus B, Saarinen M, Sauer UH, Eklund P, Johansson K, Karlsson A, Ramaswamy S, Bjork A, Synstad B, Naterstad K, Sirevag R, Eklund H, J Mol Biol. 2002 May 3;318(3):707-21. PMID:[http:// | Structural basis for thermophilic protein stability: structures of thermophilic and mesophilic malate dehydrogenases., Dalhus B, Saarinen M, Sauer UH, Eklund P, Johansson K, Karlsson A, Ramaswamy S, Bjork A, Synstad B, Naterstad K, Sirevag R, Eklund H, J Mol Biol. 2002 May 3;318(3):707-21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12054817 12054817] | ||
[[Category: Chloroflexus aurantiacus]] | [[Category: Chloroflexus aurantiacus]] | ||
[[Category: Malate dehydrogenase]] | [[Category: Malate dehydrogenase]] | ||
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[[Category: tricarboxylic acid cycle]] | [[Category: tricarboxylic acid cycle]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:28:15 2008'' | ||
Revision as of 12:28, 20 March 2008
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| , resolution 2.20Å | |||||||
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| Sites: | |||||||
| Ligands: | and | ||||||
| Activity: | Malate dehydrogenase, with EC number 1.1.1.37 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURAL BASIS FOR THERMOPHILIC PROTEIN STABILITY: STRUCTURES OF THERMOPHILIC AND MESOPHILIC MALATE DEHYDROGENASES
OverviewOverview
The three-dimensional structure of four malate dehydrogenases (MDH) from thermophilic and mesophilic phototropic bacteria have been determined by X-ray crystallography and the corresponding structures compared. In contrast to the dimeric quaternary structure of most MDHs, these MDHs are tetramers and are structurally related to tetrameric malate dehydrogenases from Archaea and to lactate dehydrogenases. The tetramers are dimers of dimers, where the structures of each subunit and the dimers are similar to the dimeric malate dehydrogenases. The difference in optimal growth temperature of the corresponding organisms is relatively small, ranging from 32 to 55 degrees C. Nevertheless, on the basis of the four crystal structures, a number of factors that are likely to contribute to the relative thermostability in the present series have been identified. It appears from the results obtained, that the difference in thermostability between MDH from the mesophilic Chlorobium vibrioforme on one hand and from the moderate thermophile Chlorobium tepidum on the other hand is mainly due to the presence of polar residues that form additional hydrogen bonds within each subunit. Furthermore, for the even more thermostable Chloroflexus aurantiacus MDH, the use of charged residues to form additional ionic interactions across the dimer-dimer interface is favored. This enzyme has a favorable intercalation of His-Trp as well as additional aromatic contacts at the monomer-monomer interface in each dimer. A structural alignment of tetrameric and dimeric prokaryotic MDHs reveal that structural elements that differ among dimeric and tetrameric MDHs are located in a few loop regions.
About this StructureAbout this Structure
1GUY is a Single protein structure of sequence from Chloroflexus aurantiacus. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for thermophilic protein stability: structures of thermophilic and mesophilic malate dehydrogenases., Dalhus B, Saarinen M, Sauer UH, Eklund P, Johansson K, Karlsson A, Ramaswamy S, Bjork A, Synstad B, Naterstad K, Sirevag R, Eklund H, J Mol Biol. 2002 May 3;318(3):707-21. PMID:12054817
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