Crystal structure of a mutant human lysozyme with a substituted disulfide bond

2001 ◽  
Vol 43 (4) ◽  
pp. 413-419 ◽  
Author(s):  
Koji Inaka ◽  
Eiko Kanaya ◽  
Masakazu Kikuchi ◽  
Kunio Miki
Keyword(s):  
Crystal Structure ◽  
Disulfide Bond ◽  
Human Lysozyme

scholarly journals Evidence for intramolecular disulfide bond shuffling in the folding of mutant human lysozyme.

1991 ◽  
Vol 266 (10) ◽  
pp. 6456-6461 ◽  
Author(s):  
Y Taniyama ◽  
R Kuroki ◽  
F Omura ◽  
C Seko ◽  
M Kikuchi
Keyword(s):  
Disulfide Bond ◽  
Human Lysozyme ◽  
Intramolecular Disulfide Bond

scholarly journals Crystal structure of an acetylesterase fromTalaromyces cellulolyticusand the importance of a disulfide bond near the active site

FEBS Letters ◽  
2015 ◽  
Vol 589 (11) ◽  
pp. 1200-1206 ◽  
Author(s):  
Masahiro Watanabe ◽  
Harumi Fukada ◽  
Hiroyuki Inoue ◽  
Kazuhiko Ishikawa
Keyword(s):  
Crystal Structure ◽  
Disulfide Bond ◽  
Active Site

scholarly journals An ultralong CDRH2 in HCV neutralizing antibody demonstrates structural plasticity of antibodies against E2 glycoprotein

eLife ◽  
2020 ◽  
Vol 9 ◽  
Author(s):  
Andrew I Flyak ◽  
Stormy E Ruiz ◽  
Jordan Salas ◽  
Semi Rho ◽  
Justin R Bailey ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Disulfide Bond ◽  
Chronic Infection ◽  
Neutralizing Antibodies ◽  
Infected Individual ◽  
Structural Plasticity ◽  
Neutralizing Antibody ◽  
Single Individual ◽  
Broadly Neutralizing Antibodies ◽  
E2 Glycoprotein

A vaccine protective against diverse HCV variants is needed to control the HCV epidemic. Structures of E2 complexes with front layer-specific broadly neutralizing antibodies (bNAbs) isolated from HCV-infected individuals, revealed a disulfide bond-containing CDRH3 that adopts straight (individuals who clear infection) or bent (individuals with chronic infection) conformation. To investigate whether a straight versus bent disulfide bond-containing CDRH3 is specific to particular HCV-infected individuals, we solved a crystal structure of the HCV E2 ectodomain in complex with AR3X, a bNAb with an unusually long CDRH2 that was isolated from the chronically-infected individual from whom the bent CDRH3 bNAbs were derived. The structure revealed that AR3X utilizes both its ultralong CDRH2 and a disulfide motif-containing straight CDRH3 to recognize the E2 front layer. These results demonstrate that both the straight and bent CDRH3 classes of HCV bNAb can be elicited in a single individual, revealing a structural plasticity of VH1-69-derived bNAbs.

scholarly journals A disulfide constrains the ToxR periplasmic domain structure, altering its interactions with ToxS and bile-salts

2020 ◽  
Author(s):  
Charles R Midgett ◽  
Rachel A Swindell ◽  
Maria Pellegrini ◽  
F Jon Kull
Keyword(s):  
Crystal Structure ◽  
Transcription Factor ◽  
Disulfide Bond ◽  
Bile Salts ◽  
Biochemical Analysis ◽  
Conformation Analysis ◽  
Binding Partner ◽  
Bile Resistance ◽  
Periplasmic Domain

AbstractToxR is a transmembrane transcription factor that, together with its integral membrane periplasmic binding partner ToxS, is conserved across the Vibrio family. In some pathogenic Vibrios, including V. parahaemolyticus and V. cholerae, ToxR is required for bile resistance and virulence, and ToxR is fully activated and protected from degradation by ToxS. ToxS achieves this in part by ensuring formation of an intra-chain disulfide bond in the C-terminal periplasmic domain of ToxR (dbToxRp). In this study, biochemical analysis showed dbToxRp to have a higher affinity for the ToxS periplasmic domain than the non-disulfide bonded conformation. Analysis of our dbToxRp crystal structure showed this is due to disulfide bond stabilization. Furthermore, dbToxRp is structurally homologous to the V. parahaemolyticus VtrA periplasmic domain. These results highlight the critical structural role of disulfide bond in ToxR and along with VtrA define a domain fold involved in environmental sensing conserved across the Vibrio family.

scholarly journals Structure of the regulatory domain of the LysR family regulator NMB2055 (MetR-like protein) fromNeisseria meningitidis

2012 ◽  
Vol 68 (7) ◽  
pp. 730-737 ◽  
Author(s):  
Sarah Sainsbury ◽  
Jingshan Ren ◽  
Nigel J. Saunders ◽  
David I. Stuart ◽  
Raymond J. Owens
Keyword(s):  
Crystal Structure ◽  
Transcription Factors ◽  
Neisseria Meningitidis ◽  
Disulfide Bond ◽  
Binding Pocket ◽  
Cysteine Residues ◽  
Regulatory Domain ◽  
High Degree ◽  
Effector Binding ◽  
Lysr Family

The crystal structure of the regulatory domain of NMB2055, a putative MetR regulator fromNeisseria meningitidis, is reported at 2.5 Å resolution. The structure revealed that there is a disulfide bond inside the predicted effector-binding pocket of the regulatory domain. Mutation of the cysteines (Cys103 and Cys106) that form the disulfide bond to serines resulted in significant changes to the structure of the effector pocket. Taken together with the high degree of conservation of these cysteine residues within MetR-related transcription factors, it is suggested that the Cys103 and Cys106 residues play an important role in the function of MetR regulators.

The Crystal Structure of Bis(2-chlorophenyl) Disulfide

1989 ◽  
Vol 42 (8) ◽  
pp. 1403 ◽  
Author(s):  
TCW Mak ◽  
WH Yip ◽  
WH Chan ◽  
G Smith ◽  
CHL Kennard
Keyword(s):  
Crystal Structure ◽  
Disulfide Bond ◽  
Torsion Angle ◽  
Monoclinic Space Group ◽  
Space Group ◽  
A Cell

The crystal structure of bis(2-chlorophenyl) disulfide has been determined and refined to a residual of 0.035 for 1573 observed reflections. Crystals are monoclinic, space group P21/a with Z 4 in a cell of dimensions a 7.724(1), b 22.360(7), c 7.917(2) � , β 114. 75�. The two chlorophenyl rings are synclinally related with a torsion angle of -85.0 � down the disulfide bond vector.

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