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1E20

The FMN binding protein AtHal3

Summary for 1E20
Entry DOI10.2210/pdb1e20/pdb
DescriptorHALOTOLERANCE PROTEIN HAL3, FLAVIN MONONUCLEOTIDE, NICKEL (II) ION, ... (5 entities in total)
Functional Keywordsflavoprotein, regulation, signal transduction, stress
Biological sourceARABIDOPSIS THALIANA (MOUSE-EAR CRESS)
Total number of polymer chains1
Total formula weight23974.01
Authors
Albert, A.,Martinez-Ripoll, M.,Espinosa-Ruiz, A.,Yenush, L.,Culianez-Macia, F.A.,Serrano, R. (deposition date: 2000-05-12, release date: 2000-09-11, Last modification date: 2025-04-09)
Primary citationAlbert, A.,Martinez-Ripoll, M.,Espinosa-Ruiz, A.,Yenush, L.,Culianez-Macia, F.A.,Serrano, R.
The X-Ray Structure of the Fmn-Binding Protein Athal3 Provides the Structural Basis for the Activity of a Regulatory Subunit Involved in Signal Transduction
Structure, 8:961-, 2000
Cited by
PubMed Abstract: The Arabidopsis thaliana HAL3 gene product encodes for an FMN-binding protein (AtHal3) that is related to plant growth and salt and osmotic tolerance. AtHal3 shows sequence homology to ScHal3, a regulatory subunit of the Saccharomyces cerevisae serine/threonine phosphatase PPz1. It has been proposed that AtHal3 and ScHal3 have similar roles in cellular physiology, as Arabidopsis transgenic plants that overexpress AtHal3 and yeast cells that overexpress ScHal3 display similar phenotypes of improved salt tolerance. The enzymatic activity of AtHal3 has not been investigated. However, the AtHal3 sequence is homologous to that of EpiD, a flavoprotein from Staphylococcus epidermidis that recognizes a peptidic substrate and subsequently catalyzes the alpha, beta-dehydrogenation of its C-terminal cysteine residue.
PubMed: 10986463
DOI: 10.1016/S0969-2126(00)00187-8
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.02 Å)
Structure validation

237735

數據於2025-06-18公開中

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