1HLP

STRUCTURAL FEATURES STABILIZING HALOPHILIC MALATE DEHYDROGENASE FROM AN ARCHAEBACTERIUM

Summary for 1HLP

• Entry DOI: 10.2210/pdb1hlp/pdb
• Descriptor: MALATE DEHYDROGENASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (2 entities in total)
• Functional Keywords: dehydrogenase, halophilic
• Biological source: Haloarcula marismortui
• Cellular location: Cytoplasm: Q07841
• Total number of polymer chains: 2
• Total formula weight: 66739.91

Authors

Dym, O.,Mevarech, M.,Sussman, J.L. (deposition date: 1994-10-04, release date: 1995-01-26, Last modification date: 2024-02-07)

Primary citation

Dym, O.,Mevarech, M.,Sussman, J.L.
Structural Features That Stabilize Halophilic Malate Dehydrogenase from an Archaebacterium.
Science, 267:1344-1346, 1995

PubMed Abstract: The high-resolution structure of halophilic malate dehydrogenase (hMDH) from the archaebacterium Haloarcula marismortui was determined by x-ray crystallography. Comparison of the three-dimensional structures of hMDH and its nonhalophilic congeners reveals structural features that may promote the stability of hMDH at high salt concentrations. These features include an excess of acidic over basic residues distributed on the enzyme surface and more salt bridges present in hMDH compared with its nonhalophilic counterparts. Other features that contribute to the stabilization of thermophilic lactate dehydrogenase and thermophilic MDH-the incorporation of alanine into alpha helices and the introduction of negatively charged amino acids near their amino termini, both of which stabilize the alpha helix as a result of interaction with the positive part of the alpha-helix dipole-also were observed in hMDH.

PubMed: 17812611
DOI: 10.1126/science.267.5202.1344

Experimental method

X-RAY DIFFRACTION (3.2 Å)