scholarly journals Cytochrome c3fromDesulfovibrio gigas: Crystal structure at 1.8 Å resolution and evidence for a specific calcium-binding site

1996 ◽  
Vol 5 (7) ◽  
pp. 1342-1354 ◽  
Author(s):  
Pedro M. Matias ◽  
José Morais ◽  
Ricardo Coelho ◽  
Maria Arménia Carrondo ◽  
Keith Wilson ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Binding Site ◽  
Calcium Binding ◽  
Calcium Binding Site

scholarly journals Crystal structure of calcium dodecin (Rv0379), from Mycobacterium tuberculosis with a unique calcium-binding site

2011 ◽  
Vol 20 (5) ◽  
pp. 827-833 ◽  
Author(s):  
Arulandu Arockiasamy ◽  
Anup Aggarwal ◽  
Christos G. Savva ◽  
Andreas Holzenburg ◽  
James C. Sacchettini
Keyword(s):  
Crystal Structure ◽  
Mycobacterium Tuberculosis ◽  
Binding Site ◽  
Calcium Binding ◽  
Calcium Binding Site

scholarly journals The X-ray structure of human calbindin-D28K: an improved model

2018 ◽  
Vol 74 (10) ◽  
pp. 1008-1014 ◽  
Author(s):  
James W. Noble ◽  
Rehab Almalki ◽  
S. Mark Roe ◽  
Armin Wagner ◽  
Ramona Duman ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Binding Site ◽  
Calcium Binding ◽  
Tertiary Structure ◽  
Nmr Structure ◽  
Calcium Binding Site ◽  
Globular Structure ◽  
Saxs Data ◽  
X Ray ◽  
Calbindin D28k

Calbindin-D28K is a widely expressed calcium-buffering cytoplasmic protein that is involved in many physiological processes. It has been shown to interact with other proteins, suggesting a role as a calcium sensor. Many of the targets of calbindin-D28K are of therapeutic interest: for example, inositol monophosphatase, the putative target of lithium therapy in bipolar disorder. Presented here is the first crystal structure of human calbindin-D28K. There are significant deviations in the tertiary structure when compared with the NMR structure of rat calbindin-D28K (PDB entry 2g9b), despite 98% sequence identity. Small-angle X-ray scattering (SAXS) indicates that the crystal structure better predicts the properties of calbindin-D28K in solution compared with the NMR structure. Here, the first direct visualization of the calcium-binding properties of calbindin-D28K is presented. Four of the six EF-hands that make up the secondary structure of the protein contain a calcium-binding site. Two distinct conformations of the N-terminal EF-hand calcium-binding site were identified using long-wavelength calcium single-wavelength anomalous dispersion (SAD). This flexible region has previously been recognized as a protein–protein interaction interface. SAXS data collected in both the presence and absence of calcium indicate that there are no large structural differences in the globular structure of calbindin-D28K between the calcium-loaded and unloaded proteins.

scholarly journals A disulfide bridge in the calcium binding site of a polyester hydrolase increases its thermal stability and activity against polyethylene terephthalate

FEBS Open Bio ◽  
2016 ◽  
Vol 6 (5) ◽  
pp. 425-432 ◽  
Author(s):  
Johannes Then ◽  
Ren Wei ◽  
Thorsten Oeser ◽  
André Gerdts ◽  
Juliane Schmidt ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Binding Site ◽  
Polyethylene Terephthalate ◽  
Calcium Binding ◽  
Disulfide Bridge ◽  
Calcium Binding Site

Calcium-Binding Site β2, Adjacent to the “b” Polymerization Site, Modulates Lateral Aggregation of Protofibrils during Fibrin Polymerization†,‡

Biochemistry ◽  
2004 ◽  
Vol 43 (9) ◽  
pp. 2475-2483 ◽  
Author(s):  
Michael S. Kostelansky ◽  
Karim C. Lounes ◽  
Li Fang Ping ◽  
Sarah K. Dickerson ◽  
Oleg V. Gorkun ◽  
...  
Keyword(s):  
Binding Site ◽  
Calcium Binding ◽  
Calcium Binding Site ◽  
Fibrin Polymerization

scholarly journals The calcium-binding site of human glutamate carboxypeptidase II is critical for dimerization, thermal stability, and enzymatic activity

2018 ◽  
Vol 27 (9) ◽  
pp. 1575-1584 ◽  
Author(s):  
Jakub Ptacek ◽  
Jana Nedvedova ◽  
Michal Navratil ◽  
Barbora Havlinova ◽  
Jan Konvalinka ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Enzymatic Activity ◽  
Binding Site ◽  
Calcium Binding ◽  
Calcium Binding Site ◽  
Glutamate Carboxypeptidase Ii ◽  
Glutamate Carboxypeptidase
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