4qwo | pdb_00004qwo

1.52 Angstrom Crystal Structure of A42R Profilin-like Protein from Monkeypox Virus Zaire-96-I-16

spinqualitylabelsall models 4qwo, resolution 1.52Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4qwo is a 2 chain structure with sequence from Monkeypox virus Zaire-96-I-16. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.52Å Ligands: CL, EDO, MSE, PE8, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PROF_MONPZ More likely to influence phosphoinositide metabolism than actin assembly. Publication Abstract from PubMed The infectious disease human monkeypox is spreading rapidly in 2022, causing a global health crisis. The genomics of Monkeypox virus (MPXV) have been extensively analyzed and reported, although little is known about the virus-encoded proteome. In particular, there are no reported experimental MPXV protein structures other than computational models. Here, a 1.52 A resolution X-ray structure of the MPXV protein A42R, the first MPXV-encoded protein with a known structure, is reported. A42R shows structural similarity to profilins, which are cellular proteins that are known to function in the regulation of actin cytoskeletal assembly. However, structural comparison of A42R with known members of the profilin family reveals critical differences that support prior biochemical findings that A42R only weakly binds actin and does not bind poly(L-proline). In addition, the analysis suggests that A42R may make distinct interactions with phosphatidylinositol lipids. Overall, the data suggest that the role of A42R in the replication of orthopoxviruses may not be readily determined by comparison to cellular profilins. Furthermore, these findings support the need for increased efforts to determine high-resolution structures of other MPXV proteins to inform physiological studies of the poxvirus infection cycle and to reveal potential new strategies to combat human monkeypox should this emerging infectious disease with pandemic potential become more common in the future. Structure of the Monkeypox virus profilin-like protein A42R reveals potential functional differences from cellular profilins.,Minasov G, Inniss NL, Shuvalova L, Anderson WF, Satchell KJF Acta Crystallogr F Struct Biol Commun. 2022 Oct 1;78(Pt 10):371-377. doi: , 10.1107/S2053230X22009128. Epub 2022 Sep 26. PMID:36189721 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Profilin 3D Structures

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