Variable Active Site Loop Conformations Accommodate the Binding of Macrocyclic Largazole Analogues to HDAC8
نویسندگان
چکیده
منابع مشابه
Reconstituted IMPDH polymers accommodate both catalytically active and inactive conformations
Several metabolic enzymes undergo reversible polymerization into macromolecular assemblies. The function of these assemblies is often unclear but in some cases they regulate enzyme activity and metabolic homeostasis. The guanine nucleotide biosynthetic enzyme inosine monophosphate dehydrogenase (IMPDH) forms octamers that polymerize into helical chains. In mammalian cells, IMPDH filaments can a...
متن کاملRelative stability of the open and closed conformations of the active site loop of streptavidin.
The eight-residue surface loop, 45-52 (Ser, Ala, Val, Gly, Asn, Ala, Glu, Ser), of the homotetrameric protein streptavidin has a "closed" conformation in the streptavidin-biotin complex, where the corresponding binding affinity is one of the strongest found in nature (ΔG ∼ -18 kcal∕mol). However, in most of the crystal structures of apo (unbound) streptavidin, the loop conformation is "open" an...
متن کاملCatalytic Cys Variable loop insertions Non - covalent Ublp binding site
A one-paragraph abstractconsisting of no more than 250words (200 words in Policy Forumessays) must be included. It shouldstate the purpose of the study, basicprocedures used, main findings, andconclusions. Abbreviations. All nonstandardabbreviations must be listed inalphabetical order, giving eachabbrevia t ion fo l lowed by i t sspelled-out version. Spel...
متن کاملDifferential Active Site Loop Conformations Mediate Promiscuous Activities in the Lactonase SsoPox
Enzymes are proficient catalysts that enable fast rates of Michaelis-complex formation, the chemical step and products release. These different steps may require different conformational states of the active site that have distinct binding properties. Moreover, the conformational flexibility of the active site mediates alternative, promiscuous functions. Here we focused on the lactonase SsoPox ...
متن کاملThe identity of the active site of oxalate decarboxylase and the importance of the stability of active-site lid conformations.
Oxalate decarboxylase (EC 4.1.1.2) catalyses the conversion of oxalate into carbon dioxide and formate. It requires manganese and, uniquely, dioxygen for catalysis. It forms a homohexamer and each subunit contains two similar, but distinct, manganese sites termed sites 1 and 2. There is kinetic evidence that only site 1 is catalytically active and that site 2 is purely structural. However, the ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochemistry
سال: 2015
ISSN: 0006-2960,1520-4995
DOI: 10.1021/acs.biochem.5b00010