1b8p
From Proteopedia
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| - | [[Image:1b8p.gif|left|200px]] | + | [[Image:1b8p.gif|left|200px]] |
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| - | '''MALATE DEHYDROGENASE FROM AQUASPIRILLUM ARCTICUM''' | + | {{Structure |
| + | |PDB= 1b8p |SIZE=350|CAPTION= <scene name='initialview01'>1b8p</scene>, resolution 1.9Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''MALATE DEHYDROGENASE FROM AQUASPIRILLUM ARCTICUM''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1B8P is a [ | + | 1B8P is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aquaspirillum_arcticum Aquaspirillum arcticum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B8P OCA]. |
==Reference== | ==Reference== | ||
| - | Structural basis for cold adaptation. Sequence, biochemical properties, and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillium arcticum., Kim SY, Hwang KY, Kim SH, Sung HC, Han YS, Cho Y, J Biol Chem. 1999 Apr 23;274(17):11761-7. PMID:[http:// | + | Structural basis for cold adaptation. Sequence, biochemical properties, and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillium arcticum., Kim SY, Hwang KY, Kim SH, Sung HC, Han YS, Cho Y, J Biol Chem. 1999 Apr 23;274(17):11761-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10206992 10206992] |
[[Category: Aquaspirillum arcticum]] | [[Category: Aquaspirillum arcticum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: dehydrogenase]] | [[Category: dehydrogenase]] | ||
| - | ''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 10:07:43 2008'' |
Revision as of 08:07, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
MALATE DEHYDROGENASE FROM AQUASPIRILLUM ARCTICUM
Overview
Aquaspillium arcticum is a psychrophilic bacterium that was isolated from arctic sediment and grows optimally at 4 degrees C. We have cloned, purified, and characterized malate dehydrogenase from A. arcticum (Aa MDH). We also have determined the crystal structures of apo-Aa MDH, Aa MDH.NADH binary complex, and Aa MDH.NAD.oxaloacetate ternary complex at 1.9-, 2.1-, and 2.5-A resolutions, respectively. The Aa MDH sequence is most closely related to the sequence of a thermophilic MDH from Thermus flavus (Tf MDH), showing 61% sequence identity and over 90% sequence similarity. Stability studies show that Aa MDH has a half-life of 10 min at 55 degrees C, whereas Tf MDH is fully active at 90 degrees C for 1 h. Aa MDH shows 2-3-fold higher catalytic efficiency compared with a mesophilic or a thermophilic MDH at the temperature range 4-10 degrees C. Structural comparison of Aa MDH and Tf MDH suggests that the increased relative flexibility of active site residues, favorable surface charge distribution for substrate and cofactor, and the reduced intersubunit ion pair interactions may be the major factors for the efficient catalytic activity of Aa MDH at low temperatures.
About this Structure
1B8P is a Single protein structure of sequence from Aquaspirillum arcticum. Full crystallographic information is available from OCA.
Reference
Structural basis for cold adaptation. Sequence, biochemical properties, and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillium arcticum., Kim SY, Hwang KY, Kim SH, Sung HC, Han YS, Cho Y, J Biol Chem. 1999 Apr 23;274(17):11761-7. PMID:10206992
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