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Proteins are organic compounds made of amino acids arranged in a linear chain and
joined together by peptide bonds between the carboxyl and amino groups of adjacent
amino acid residues. The sequence of amino acids in a protein is defined by the sequence
of a gene, which is encoded in the genetic code. In general, the genetic code specifies 20
standard amino acids, however in certain organisms the genetic code can include
selenocysteine - and in certain archaea - pyrrolysine. The residues in a protein are often
observed to be chemically modified by post-translational modification, which can happen
either before the protein is used in the cell, or as part of control mechanisms. Proteins can
also work together to achieve a particular function, and they often associate to form
stable complexes.
Like other biological macromolecules such as polysaccharides and nucleic acids, proteins
are essential parts of organisms and participate in every process within cells. Many
proteins are enzymes that catalyze biochemical reactions and are vital to metabolism.
Proteins also have structural or mechanical functions, such as actin and myosin in muscle
and the proteins in the cytoskeleton, which form a system of scaffolding that maintains
cell shape. Other proteins are important in cell signaling, immune responses, cell
adhesion, and the cell cycle. Proteins are also necessary in animals' diets, since animals
cannot synthesize all the amino acids they need and must obtain essential amino acids
from food. Through the process of digestion, animals break down ingested protein into
free amino acids that are then used in metabolism
Many small bacterial, archaebacterial, and eukaryotic genomes have been sequenced, and
the larger eukaryotic genomes are predicted to be completely sequenced within the next
decade. In all genomes sequenced to date, a large portion of these organisms’ predicted
protein coding regions encode polypeptides of unknown biochemical, biophysical, and/or
cellular functions. Three-dimensional structures of these proteins may suggest
biochemical or biophysical functions. Here we report the crystal structure of one such
protein, MJ0577, from a hyperthermophile, Methanococcus jannaschii , at 1.7-Å
resolution. The structure contains a bound ATP, suggesting MJ0577 is an ATPase or an
ATP-mediated molecular switch, which we confirm by biochemical experiments.
Furthermore, the structure reveals different ATP binding motifs that are shared among
many homologous hypothetical proteins in this family. This result indicates that
structure-based assignment of molecular function is a viable approach for the large-scale
biochemical assignment of proteins and for discovering new motifs, a basic premise of
structural genomics.
• Glycolysis
• Πηοτοσψντηεσισ
• Πηοσπηορψλατιον
• Χοντρολ οφ ηορµονεσ
• ∆ΝΑ µεταβολισµ
• ΡΝΑ µεταβολισµ
• Προτειν µεταβολισµ
• Γλοβιν προτειν
Οτηερσ
Glycolysis
• Alcohol dehydrogenase class IV sigma chain [Homo sapiens (human)]:
PDB:1D1S
Photosynthesis
• ATP synthase (F0 portion) [Escherichia coli (bacteria)]: PDB:1C17
The best-known role of proteins in the cell is as enzymes, which catalyze chemical
reactions. Enzymes are usually highly specific and accelerate only one or a few chemical
reactions. Enzymes carry out most of the reactions involved in metabolism, as well as
manipulating DNA in processes such as DNA replication, DNA repair, and transcription.
Some enzymes act on other proteins to add or remove chemical groups in a process
known as post-translational modification. About 4,000 reactions are known to be
catalyzed by enzymes. The rate acceleration conferred by enzymatic catalysis is often
enormous - as much as 1017-fold increase in rate over the uncatalyzed reaction in the case
of orotate decarboxylase (78 million years without the enzyme, 18 milliseconds with the
enzyme).
The molecules bound and acted upon by enzymes are called substrates. Although
enzymes can consist of hundreds of amino acids, it is usually only a small fraction of the
residues that come in contact with the substrate, and an even smaller fraction - 3-4
residues on average - that are directly involved in catalysis.The region of the enzyme that
binds the substrate and contains the catalytic residues is known as the active site
Phosphorylation
• Protein kinase CheY/CheA complex (bacteria chemotaxis) [Escherichia coli
(bacteria)]: PDB:1A0O
Control of hormones
• Androgen receptor [Homo sapiens (human)]:
DNA metabolism
• Restriction endonuclease BamHI/DNA complex [Bacillus amyloliquefaciens
(bacteria)]: PDB:1BHM
• Restriction enzyme EcoRV / DNA Complex (after DNA cleaved, with Mg2+ ion)
[Escherichia coli (bacteria)]: PDB:1RVC
• clamp loader (RFC) bound to the DNA sliding clamp (PCNA) [Saccharomyces
cerevisiae (Baker's yeast)]: PDB:1SXJ
RNA metabolism
• Sex-lethal (Sxl) protein/RNA complex [Drosophila melanogaster (fruit fly)]:
PDB:1B7F
• Catabolite gene activator protein complex with DNA [Escherichia coli (bacteria)]:
PDB:1CGP
• Group I self-splicing intron in complex with its exons [Homo sapiens (Human)]:
PDB:1U6B
• Phage twort group I ribozyme (self-splicing intron) complexed with it's product
[Bacteriophage Twort (virus)]: PDB:1Y0Q
• The zinc finger (DNA binding site) of transcription factor Zif268/DNA complex
[Mus musculus (house mouse)]: PDB:1ZAA
Protein metabolism
• Hepatitis C virus NS3 protease [Hepatitis C virus(HCV)]: PDB:1A1R
• Simian virus 5 V protien complexed with human DDB1 [Simian virus 5 / Homo
sapiens (human)]: PDB:2B5L
• Catabolite gene activator protein complex with DNA [Escherichia coli (bacteria)]:
PDB:1CGP
Globin protein
• Myoglobin [Sperm whale]: PDB:1MBN
Others
• Immunoglobulin M rheumatoid factor Fab complexed with IgG4 Fc [Homo
sapiens (human)]: PDB:1ADQ
• Complex between T-cell receptor, viral peptide and HLA-A2 [Homo sapiens
(human)]: PDB:1AO7
• Botulinum neurotoxin type B complex with zinc ion and inhibitor (bis(5-amidino-
2-benzimidazolyl)methane) [Clostridium botulinum (bacteria)]: PDB:1G9B
• C-H-RAS P21 protein catalytic domain (wild type) [Homo sapiens (human)]
• Nerve growth factor in complex with its receptor, p75 [Homo sapiens (human)]
• Periplasmic chaperone Skp [Escherichia coli (bacteria)]
• gamma-delta T cell receptor in complex with MHC T22 [Mus musculus (house
mouse)]
• Filamin A complexed with integrin beta 7 tail fragment [Homo sapiens (human)]:
• ZEBRA protein complexed with double strand DNA [Epstein-Barr virus (EBV,
Human herpesvirus 4 (HHV-4))]