Arginine and nitrogen storage

Current Opinion in Structural Biology

Volumn 18, Issue 6, 2008, Pages 673-681

  Llácer, José L ^a   Fita, Ignacio ^b   Rubio, Vicente ^a  

^a CENTRO DE INVESTIGACIÓN BIOMÉDICA EN RED DE ENFERMEDADES RARAS CIBERER   (Spain)

^b INSTITUTE FOR RESEARCH IN BIOMEDICINE   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; NITROGEN;

BINDING AFFINITY; BINDING SITE; CRYSTAL STRUCTURE; CYANOBACTERIUM; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN STRUCTURE; REVIEW;

CYANOBACTERIA; EUKARYOTA; PROKARYOTA;

EID: 57049163521     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2008.11.002     Document Type: Review

References (49)

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20. ••]. The structures explain also why the uridylylation of the T-loop residue Tyr51 prevents PII-AmtB complex formation.
21. ••].
22. m of NAGK for NAG within the complex is attributed to PII-triggered NAG site conformational changes. NAGK relief from arginine inhibition is due to changes in the arginine site resulting from symmetry-determined changes in the overall shape of the NAGK hexamer as well as to local effects.
23. ••] are highly similar. The crystals contain MgATP bound to PII and NAG, ADP and arginine bound to NAGK. The site for the arginine inhibitor is in a low-affinity form because of the orientation of the N-terminal helices that interconnect the three dimers in the hexamer. Both NAGK subunits in the asymmetric unit exhibit different degrees of active centre opening. The movement causing this active centre change is a rotation around a hinge located at the boundary between both domains of each NAGK subunit, near the site at which the T-loop contacts NAGK. Thus, the stimulatory effect of PII on the kinetics of arginine-inhibited NAGK is attributed to a PII-limited degree of opening and closing of the active site cleft, in opposition to a domain-separating inhibitory effect exerted by arginine.
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