This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1d3a

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1d3a.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1d3a.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1d3a| PDB=1d3a | SCENE= }}
{{STRUCTURE_1d3a| PDB=1d3a | SCENE= }}
-
'''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===
-
==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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10653643}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10653643 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10653643}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Zaccai, G.]]
[[Category: Zaccai, G.]]
[[Category: Rossmann fold and 3 sorts of complex salt bridge]]
[[Category: Rossmann fold and 3 sorts of complex salt bridge]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:24:07 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:16:58 2008''

Revision as of 19:17, 30 June 2008

Image:1d3a.png

Template:STRUCTURE 1d3a

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

Template:ABSTRACT PUBMED 10653643

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 Mon Jun 30 22:16:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1d3a"
Personal tools