2hlp
From Proteopedia
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|PDB= 2hlp |SIZE=350|CAPTION= <scene name='initialview01'>2hlp</scene>, resolution 2.59Å | |PDB= 2hlp |SIZE=350|CAPTION= <scene name='initialview01'>2hlp</scene>, resolution 2.59Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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] | + | |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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hlp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hlp OCA], [http://www.ebi.ac.uk/pdbsum/2hlp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hlp RCSB]</span> | ||
}} | }} | ||
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[[Category: Richard, S B.]] | [[Category: Richard, S B.]] | ||
[[Category: Zaccai, G.]] | [[Category: Zaccai, G.]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: NA]] | ||
[[Category: halophilic]] | [[Category: halophilic]] | ||
[[Category: ion-binding]] | [[Category: ion-binding]] | ||
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[[Category: salt bridge]] | [[Category: salt bridge]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:32:04 2008'' |
Revision as of 00:32, 31 March 2008
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| , resolution 2.59Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Malate dehydrogenase, with EC number 1.1.1.37 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE E267R MUTANT OF A 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
2HLP 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
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