2hlp - Proteopedia, life in 3D

Revision as of 15:18, 20 March 2008

Image:2hlp.gif

, resolution 2.59Å

Ligands:

and

Activity:

Malate dehydrogenase, with EC number 1.1.1.37

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

Page seeded by OCA on Thu Mar 20 17:18:35 2008

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Retrieved from "http://52.214.119.220/wiki/index.php/2hlp"

@@ Line 1: / Line 1: @@
-[[Image:2hlp.gif|left|200px]]<br /><applet load="2hlp" size="350" color="white" frame="true" align="right" spinBox="true"
+[[Image:2hlp.gif|left|200px]]
-caption="2hlp, resolution 2.59&Aring;" />
-'''CRYSTAL STRUCTURE OF THE E267R MUTANT OF A HALOPHILIC MALATE DEHYDROGENASE IN THE APO FORM'''<br />
+ {{Structure
+|PDB= 2hlp |SIZE=350|CAPTION= <scene name='initialview01'>2hlp</scene>, resolution 2.59&Aring;
+|SITE=
+|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <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]
+|GENE=
+}}
+'''CRYSTAL STRUCTURE OF THE E267R MUTANT OF A HALOPHILIC MALATE DEHYDROGENASE IN THE APO FORM'''
 ==Overview==
@@ Line 7: / Line 16: @@
 ==About this Structure==
-HLP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haloarcula_marismortui Haloarcula marismortui] with <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=NA:'>NA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HLP OCA].
+HLP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Haloarcula_marismortui Haloarcula marismortui]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HLP 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10653643 10653643]
+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:[http://www.ncbi.nlm.nih.gov/pubmed/10653643 10653643]
 [[Category: Haloarcula marismortui]]
 [[Category: Malate dehydrogenase]]
@@ Line 23: / Line 32: @@
 [[Category: ion-binding]]
 [[Category: malate dehydrogenase]]
-[[Category: salt bridges]]
+[[Category: salt bridge]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:43:07 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:18:35 2008''