X-ray Crystal Structure of Alcohol Products Bound at the Active Site of Soluble Methane Monooxygenase Hydroxylase

2001 ◽  
Vol 123 (8) ◽  
pp. 1794-1795 ◽  
Author(s):  
Douglas A. Whittington ◽  
Matthew H. Sazinsky ◽  
Stephen J. Lippard
Keyword(s):  
Crystal Structure ◽  
Active Site ◽  
Methane Monooxygenase ◽  
X Ray ◽  
Soluble Methane Monooxygenase

scholarly journals High-Energy-Resolution Fluorescence-Detected X-ray Absorption of the Q Intermediate of Soluble Methane Monooxygenase

2017 ◽  
Vol 139 (49) ◽  
pp. 18024-18033 ◽  
Author(s):  
Rebeca G. Castillo ◽  
Rahul Banerjee ◽  
Caleb J. Allpress ◽  
Gregory T. Rohde ◽  
Eckhard Bill ◽  
...  
Keyword(s):  
Energy Resolution ◽  
Methane Monooxygenase ◽  
High Energy ◽  
High Energy Resolution ◽  
X Ray ◽  
Soluble Methane Monooxygenase ◽  
X Ray Absorption

scholarly journals Crystal structure of a pyridoxal 5′-phosphate-dependent aspartate racemase derived from the bivalve mollusc Scapharca broughtonii

2017 ◽  
Vol 73 (12) ◽  
pp. 651-656 ◽  
Author(s):  
Taichi Mizobuchi ◽  
Risako Nonaka ◽  
Motoki Yoshimura ◽  
Katsumasa Abe ◽  
Shouji Takahashi ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Binding Site ◽  
Active Site ◽  
Metal Binding ◽  
Bivalve Mollusc ◽  
Active Site Residues ◽  
X Ray ◽  
Aspartate Racemase ◽  
Scapharca Broughtonii

Aspartate racemase (AspR) is a pyridoxal 5′-phosphate (PLP)-dependent enzyme that is responsible for D-aspartate biosynthesis in vivo. To the best of our knowledge, this is the first study to report an X-ray crystal structure of a PLP-dependent AspR, which was resolved at 1.90 Å resolution. The AspR derived from the bivalve mollusc Scapharca broughtonii (SbAspR) is a type II PLP-dependent enzyme that is similar to serine racemase (SR) in that SbAspR catalyzes both racemization and dehydration. Structural comparison of SbAspR and SR shows a similar arrangement of the active-site residues and nucleotide-binding site, but a different orientation of the metal-binding site. Superposition of the structures of SbAspR and of rat SR bound to the inhibitor malonate reveals that Arg140 recognizes the β-carboxyl group of the substrate aspartate in SbAspR. It is hypothesized that the aromatic proline interaction between the domains, which favours the closed form of SbAspR, influences the arrangement of Arg140 at the active site.

Difference in Conformation of Virginiamycin M1 in Chloroform and Bound Form in the 50S Ribosome or Streptogramin Acetyltransferase

2004 ◽  
Vol 57 (5) ◽  
pp. 415 ◽  
Author(s):  
Jason Dang ◽  
B. Mikael Bergdahl ◽  
Frances Separovic ◽  
Robert T. C. Brownlee ◽  
Robert P. Metzger
Keyword(s):  
Crystal Structure ◽  
High Resolution ◽  
Active Site ◽  
Major Change ◽  
X Ray ◽  
Binding Process ◽  
High Resolution Nmr ◽  
Virginiamycin M1

The conformation of virginiamycin M1 (VM1) in chloroform, determined by high-resolution NMR experiments, differs significantly from that of the X-ray crystal structure of VM1 bound to the 50S ribosome and to the active site of a streptogramin acetyltransferase enzyme. This implies that the binding process to these entities causes a major change in VM1 conformation.

Influence of the presence of the heme cofactor on the JK-loop structure in indoleamine 2,3-dioxygenase 1

2020 ◽  
Vol 76 (12) ◽  
pp. 1211-1221
Author(s):  
Manon Mirgaux ◽  
Laurence Leherte ◽  
Johan Wouters
Keyword(s):  
Crystal Structure ◽  
Cancer Research ◽  
Active Site ◽  
Loop Structure ◽  
X Ray Diffraction ◽  
Dynamic Information ◽  
X Ray ◽  
Indoleamine 2,3 Dioxygenase ◽  
First Time ◽  
Heme Cofactor

Indoleamine 2,3-dioxygenase 1 has sparked interest as an immunotherapeutic target in cancer research. Its structure includes a loop, named the JK-loop, that controls the orientation of the substrate or inhibitor within the active site. However, little has been reported about the crystal structure of this loop. In the present work, the conformation of the JK-loop is determined for the first time in the presence of the heme cofactor in the active site through X-ray diffraction experiments (2.44 Å resolution). Molecular-dynamics trajectories were also obtained to provide dynamic information about the loop according to the presence of cofactor. This new structural and dynamic information highlights the importance of the JK-loop in confining the labile heme cofactor to the active site.

Explorations of the Nonheme High-Valent Iron-Oxo Landscape: Crystal Structure of a Synthetic High-valent Complex with an [FeIV2(mu-O)2] Diamond Core Relevant to the Chemistry of sMMOH

2021 ◽  
Author(s):  
Gregory T Rohde ◽  
Genqiang Xue ◽  
Lawrence Que
Keyword(s):  
Crystal Structure ◽  
Active Site ◽  
Methane Monooxygenase ◽  
Methanotrophic Bacteria ◽  
High Valent ◽  
Soluble Enzymes

Methanotrophic bacteria utilize methane monooxygenase (MMO) to carry out the first step in metabolizing methane. The soluble enzymes employ a hydroxylase component (sMMOH) with a nonheme diiron active site that...

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