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<StructureSection load='1j1v' size='340' side='right' caption='DNA.' scene=''>
<StructureSection load='1j1v' size='340' side='right' caption='DNA.' scene=''>
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<scene name='75/751151/Dna_molecule/2'>This is my DNA.</scene>
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<scene name='75/751151/Area_of_interaction/1'>area of interaction with DNA</scene>
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== Structural highlights ==
== Structural highlights ==
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DnaA has <scene name="/12/3456/Sample/1">one unique protein chain</scene> and two unique <scene name="/12/3456/Sample/2">nucleic acid chains</scene>.
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DnaA has <scene name='75/751151/One_unique_protein_chain/1'>one unique protein chain</scene> and <scene name='75/751151/Two_unique_nucleic_acid_chains/1'>two unique nucleic acid chains</scene>.
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The unique protein chain, chromosomal replication initiator protein dnaA (gene name: dnaA b3702 JW3679), assists in the regulation and regulation of chromosomal replication. Its function is ATP dependent, so it is only able to assist in replication once per cell cycle.
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</StructureSection>
</StructureSection>
== References ==
== References ==
<references/>
<references/>
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http://www.rcsb.org/pdb/explore.do?structureId=1j1v

Revision as of 21:22, 7 February 2017

Contents

genetics is ok

'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. 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.

'Function"

The protein complex participates in placing the amino acids in their correct order when messenger RNA is translated into a protein sequence on the ribosome by promoting GTP-dependent binding of tRNA to the A site of the ribosome. In other words, it is involved with elongation during polypeptide synthesis.

Phe-tRNA, elongation factor EF-TU:GDPNP Ternary complex

Drag the structure with the mouse to rotate

DNA.

Drag the structure with the mouse to rotate

References

  1. Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644

http://www.rcsb.org/pdb/explore.do?structureId=1j1v

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