2hp1 | pdb_00002hp1

Inter-subunit signaling in GSAM

spinqualitylabelsall models 2hp1, resolution 2.08Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2hp1 is a 2 chain structure with sequence from Anacystis nidulans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EA5, HOZ, PLP Related: 2hoy, 2hoz, 2hp2 Gene: hemL, gsa (Anacystis nidulans) Activity: Glutamate-1-semialdehyde 2,1-aminomutase, with EC number 5.4.3.8 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 Enzymes are highly dynamic and tightly controlled systems. However, allosteric communication linked to catalytic turnover is poorly understood. We have performed an integrated approach to trap several catalytic intermediates in the alpha2-dimeric key enzyme of chlorophyll biosynthesis, glutamate-1-semialdehyde aminomutase. Our data reveal an active-site "gating loop," which undergoes a dramatic conformational change during catalysis, that is simultaneously open in one subunit and closed in the other. This loop movement requires a beta-sheet-to-alpha-helix transition to assume the closed conformation, thus facilitating transport of substrate toward, and concomitantly forming, an integral part of the active site. The accompanying intersubunit cross-talk, which controls negative cooperativity between the allosteric pair, was explored at the atomic level. The central elements of the communication triad are the cofactor bound to different catalytic intermediates, the interface helix, and the gating loop. Together, they form a molecular switch in which the cofactor acts as a central signal transmitter linking the subunit interface with the gating loop. Intersubunit signaling in glutamate-1-semialdehyde-aminomutase.,Stetefeld J, Jenny M, Burkhard P Proc Natl Acad Sci U S A. 2006 Sep 12;103(37):13688-93. Epub 2006 Sep 5. PMID:16954186 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aminomutase 3D structures

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