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Heterodimer </scene> alignment.

Specific are highlighted here. The ligands listed above, GDP, Phe, and Mg+2 ion each attach at these locations which are still being explored.

which play a crucial role in binding to the ribosome during translation. They form positive pockets with which negative amino acids can bind to.

'Molecules it Interacts With and where '

The protein binds to GDP as well as the following ligands in order to promote the attachment of the protein complex to the ribosome A site.

PHOSHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER

PHENYLALANINE MAGNESIUM ION

'Origin'

It has domains that are created in yeast (phenyl-transfer RNA) , in the heat resistant Thermus aquaticus (EF-Tu elongation factor, and can be synthetically manufactured.

'Structure'

It has 3 domains. G proteins, Elongation Factors, and the EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain. It is composed of 6 chains, which combine in alignment.

Specific are highlighted here.

which play a crucial role in binding to the ribosome during translation.

Topoisomerase I is an enzyme that winds and unwinds the DNA double helix in order to increase or decrease supercoiling. By controlling supercoiling, topoisomerase indirectly controls DNA transcription, as a highly supercoiled molecule is difficult to transcribe while a relaxed helix is easier to access. This enzyme exists in both prokaryotes and eukaryotes.

Function

The on the topoisomerase are responsible for catalyzing the phosphodiester cleavage reactions.

1. Topoisomerase binds to DNA and cuts one strand while simultaneously forming a covalent phosphoester bond b/w the 5’ end of the cut DNA strand one of topoisomerase’s tyrosine residues.

2. Topoisomerase holds the free 3’ end of cut DNA noncovalently. 3. The non-cleaved DNA strand is passed through the cleaved ends. 4. The cleaved strand is reattached, unwinding the helix.

Structural highlights

Topoisomerase is a single protein chain consisting of . It can be separated into four domains. Domain I has 1 beta pleated sheet and 4 alpha helices, and is most likely responsible for binding topoisomerase to DNA. Domain II is made up of 2 beta pleated sheets and 1 alpha helix. Domain III is made up of 5 alpha helices, and it contains , which is the catalytic part of tyrosine's active site. Domain IV contains 8 alpha helices, and it is most likely responsible for providing the overall structure and support of topoisomerase.

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.