2hlp

From Proteopedia

(Difference between revisions)

Current revision

CRYSTAL STRUCTURE OF THE E267R MUTANT OF A HALOPHILIC MALATE DEHYDROGENASE IN THE APO FORM

Structural highlights

2hlp is a 2 chain structure with sequence from Haloarcula marismortui. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.59Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MDH_HALMA Catalyzes the reversible oxidation of malate to oxaloacetate.[HAMAP-Rule:MF_00487]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Richard SB, Madern D, Garcin E, Zaccai G. 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. Biochemistry. 2000 Feb 8;39(5):992-1000. PMID:10653643

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:2hlp.png|left|200px]]
-<!--
+==CRYSTAL STRUCTURE OF THE E267R MUTANT OF A HALOPHILIC MALATE DEHYDROGENASE IN THE APO FORM==
-The line below this paragraph, containing "STRUCTURE_2hlp", creates the "Structure Box" on the page.
+<StructureSection load='2hlp' size='340' side='right'caption='[[2hlp]], [[Resolution|resolution]] 2.59&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2hlp]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HLP FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.59&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-{{STRUCTURE_2hlp|  PDB=2hlp  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hlp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hlp OCA], [https://pdbe.org/2hlp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hlp RCSB], [https://www.ebi.ac.uk/pdbsum/2hlp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hlp ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/MDH_HALMA MDH_HALMA] Catalyzes the reversible oxidation of malate to oxaloacetate.[HAMAP-Rule:MF_00487]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hl/2hlp_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2hlp ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-===CRYSTAL STRUCTURE OF THE E267R MUTANT OF A HALOPHILIC MALATE DEHYDROGENASE IN THE APO FORM===
+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<ref>PMID:10653643</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2hlp" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_10653643}}, adds the Publication Abstract to the page
+*[[Malate Dehydrogenase 3D structures|Malate Dehydrogenase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 10653643 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_10653643}}
+__TOC__
+</StructureSection>
-==About this Structure==
-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://www.ncbi.nlm.nih.gov/pubmed/10653643 10653643]
 [[Category: Haloarcula marismortui]]
-[[Category: Malate dehydrogenase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Garcin E]]
-[[Category: Garcin, E.]]
+[[Category: Madern D]]
-[[Category: Madern, D.]]
+[[Category: Richard SB]]
-[[Category: Richard, S B.]]
+[[Category: Zaccai G]]
-[[Category: Zaccai, G.]]
-[[Category: Halophilic]]
-[[Category: Ion-binding]]
-[[Category: Malate dehydrogenase]]
-[[Category: Salt bridge]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 01:40:47 2008''

2hlp

From Proteopedia

Current revision

CRYSTAL STRUCTURE OF THE E267R MUTANT OF A HALOPHILIC MALATE DEHYDROGENASE IN THE APO FORM

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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