Structural highlights
Function
[NP4_RHOPR] Heme-based protein that deliver nitric oxide gas (NO) to the victim while feeding, resulting in vasodilation and inhibition of platelet aggregation. Also bind tightly to histamine, which is released by the host to induce wound healing (By similarity).
Publication Abstract from PubMed
Prestidigitation: In a mutant of the heme protein nitrophorin 4, the first binding of guanidine to iron in a porphyrin is observed. The protein pocket has two effects that aid this binding: its overall structure holds the ligands together providing binding energy from the chelate effect and it facilitates the deprotonation of the highly basic guanidine residue.
Guanidine-Ferroheme Coordination in the Mutant Protein Nitrophorin 4(L130R).,He C, Fuchs MR, Ogata H, Knipp M Angew Chem Int Ed Engl. 2012 Apr 27;51(18):4470-3. doi: 10.1002/anie.201108691., Epub 2012 Feb 14. PMID:22334402[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ He C, Fuchs MR, Ogata H, Knipp M. Guanidine-Ferroheme Coordination in the Mutant Protein Nitrophorin 4(L130R). Angew Chem Int Ed Engl. 2012 Apr 27;51(18):4470-3. doi: 10.1002/anie.201108691., Epub 2012 Feb 14. PMID:22334402 doi:10.1002/anie.201108691
