About: X‐ray crystallographic determination of the structure of the influenza C virus haemagglutinin‐esterase‐fusion glycoprotein

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About: X‐ray crystallographic determination of the structure of the influenza C virus haemagglutinin‐esterase‐fusion glycoprotein Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	X‐ray crystallographic determination of the structure of the influenza C virus haemagglutinin‐esterase‐fusion glycoprotein
Creator	Wong, Chi-Huey Zhang, Xiaodong Skehel, John Meier-Ewert, H Fitz, Wolfgang Rosenthal, Peter Formanowski, ³ Wiley, Don
Source	Medline; PMC
abstract	The structure of the haemagglutinin‐esterase‐fusion (HEF) glycoprotein from influenza C virus has been determined to 3.2 Å resolution by X‐ray crystallography. A synthetic mercury‐containing esterase inhibitor and receptor analogue, 9‐acetamidosialic acid α‐thiomethylmercuryglycoside, was designed as the single isomorphous heavy‐atom derivative. The asymmetric unit of one crystal form (form I; P4(3)22, a = b = 155.4, c = 414.4 Å) contained an HEF trimer. Six mercury sites identifying the three haemagglutination and three esterase sites were located by difference Patterson map analysis of a 6.5 Å resolution derivative data set. These positions defined the molecular threefold‐symmetry axis of the HEF trimer. A molecular envelope was defined by averaging a 7.0 Å resolution electron‐density map, phased by single isomorphous replacement (SIR), about the non‐crystallographic threefold‐symmetry axis. Iterative non‐crystallographic symmetry averaging in real space, solvent flattening and histogram matching were used to extend the phases to 3.5 Å resolution. Molecular replacement of the model into a second crystal form (form II; P4(3)2(1)2, a = b = 217.4, c = 421.4 Å) containing two HEF trimers per asymmetric unit permitted iterative ninefold averaging of the electron density. The 3.5 Å electron‐density map allowed an unambiguous tracing of the polypeptide chain and identification of N‐linked carbohydrates. The model has been refined by least squares to 3.2 Å resolution (R (free) = 26.7%).
has issue date	2007-09-27(xsd:dateTime)
bibo:doi	10.1107/s0907444999000232
bibo:pmid	10216291
has license	no-cc
sha1sum (hex)	9120ffe443d40980ed06e63ecc9afe7890e7fe8a
schema:url	https://doi.org/10.1107/s0907444999000232
resource representing a document's title	X‐ray crystallographic determination of the structure of the influenza C virus haemagglutinin‐esterase‐fusion glycoprotein
has PubMed Central identifier	PMC7161583
has PubMed identifier	10216291
schema:publication	Acta Crystallogr D Biol Crystallogr
resource representing a document's body	covid:9120ffe443d40980ed06e63ecc9afe7890e7fe8a#body_text
is schema:about of	named entity 'Biological' named entity 'RESEARCH' named entity 'FUSION PROTEIN' named entity 'glycoprotein' named entity 'protein' named entity 'crystallographic' named entity 'esterase' named entity 'X-ray crystallographic' named entity 'esterase' named entity 'esterase' named entity 'molecule' named entity 'electron density' named entity 'active-site' named entity 'virus' named entity 'molecular model' named entity '3.5' named entity 'X-ray diffraction' named entity 'dashed' named entity 'N-terminal' named entity 'active-site' named entity 'trimer' named entity 'crystal form' named entity 'enzyme' named entity 'electron density' named entity 'polypeptide chain' named entity 'cell receptor' named entity 'glycoprotein' named entity 'electron density' named entity 'molecule' named entity 'N-linked' named entity 'X-PLOR' named entity 'trimers' named entity 'post-translationally' named entity 'mercury' named entity 'trimer' named entity 'annealing' named entity 'N-terminal' named entity 'solvent' named entity 'Correlation' named entity 'inhibition constant' named entity 'trimer' named entity 'acetyl group' named entity 'pandemics' named entity 'electron density' named entity 'viral entry' named entity 'polypeptide' named entity 'binding site' named entity 'electron density' named entity 'glycoproteins' named entity 'trimer' named entity 'B-factor' named entity 'electron density' named entity 'virus' named entity 'trimer' named entity 'Electron density' named entity 'enzyme' named entity 'sequence identity' named entity 'infectivity' named entity 'glycoprotein' named entity 'electron density' named entity '3.5' named entity 'enzyme' named entity '3.5' named entity 'correlation' named entity 'rigid body' named entity 'Crystallization' named entity 'protein' named entity 'receptor sites' named entity 'electrostatic charge' named entity 'Electron density' named entity 'evolution' named entity '3.5' named entity 'binding pocket' named entity 'cell receptor'

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About: X‐ray crystallographic determination of the ­structure of the influenza C virus haemagglutinin‐esterase‐fusion glycoprotein Goto Sponge NotDistinct Permalink

About: X‐ray crystallographic determination of the structure of the influenza C virus haemagglutinin‐esterase‐fusion glycoprotein Goto Sponge NotDistinct Permalink