1d3a

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[[Image:1d3a.gif|left|200px]]
[[Image:1d3a.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1d3a |SIZE=350|CAPTION= <scene name='initialview01'>1d3a</scene>, resolution 2.94&Aring;
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The line below this paragraph, containing "STRUCTURE_1d3a", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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{{STRUCTURE_1d3a| PDB=1d3a | SCENE= }}
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|RELATEDENTRY=[[2hlp|2hlp]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1d3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d3a OCA], [http://www.ebi.ac.uk/pdbsum/1d3a PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1d3a RCSB]</span>
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}}
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'''CRYSTAL STRUCTURE OF THE WILD TYPE HALOPHILIC MALATE DEHYDROGENASE IN THE APO FORM'''
'''CRYSTAL STRUCTURE OF THE WILD TYPE HALOPHILIC MALATE DEHYDROGENASE IN THE APO FORM'''
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[[Category: Richard, S B.]]
[[Category: Richard, S B.]]
[[Category: Zaccai, G.]]
[[Category: Zaccai, G.]]
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[[Category: rossmann fold and 3 sorts of complex salt bridge]]
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[[Category: Rossmann fold and 3 sorts of complex salt bridge]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:24:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:33:47 2008''
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Revision as of 10:24, 2 May 2008

Image:1d3a.gif

Template:STRUCTURE 1d3a

CRYSTAL STRUCTURE OF THE WILD TYPE HALOPHILIC MALATE DEHYDROGENASE IN THE APO FORM


Overview

Previous biophysical studies of tetrameric malate dehydrogenase from the halophilic archaeon Haloarcula marismortui (Hm MalDH) have revealed the importance of protein-solvent interactions for its adaptation to molar salt conditions that strongly affect protein solubility, stability, and activity, in general. The structures of the E267R stability mutant of apo (-NADH) Hm MalDH determined to 2.6 A resolution and of apo (-NADH) wild type Hm MalDH determined to 2.9 A resolution, presented here, highlight a variety of novel protein-solvent features involved in halophilic adaptation. The tetramer appears to be stabilized by ordered water molecule networks and intersubunit complex salt bridges "locked" in by bound solvent chloride and sodium ions. The E267R mutation points into a central ordered water cavity, disrupting protein-solvent interactions. The analysis of the crystal structures showed that halophilic adaptation is not aimed uniquely at "protecting" the enzyme from the extreme salt conditions, as may have been expected, but, on the contrary, consists of mechanisms that harness the high ionic concentration in the environment.

About this Structure

1D3A is a Single protein structure of sequence from Haloarcula marismortui. Full crystallographic information is available from OCA.

Reference

Halophilic adaptation: novel solvent protein interactions observed in the 2.9 and 2.6 A resolution structures of the wild type and a mutant of malate dehydrogenase from Haloarcula marismortui., Richard SB, Madern D, Garcin E, Zaccai G, Biochemistry. 2000 Feb 8;39(5):992-1000. PMID:10653643 Page seeded by OCA on Fri May 2 13:24:07 2008

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