Sandbox Reserved 1697

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== Function of your protein ==
== Function of your protein ==
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The function of 7KIR is dephosphorylating inositol, the substrate is IP2 and the product is IP.
== Biological relevance and broader implications ==
== Biological relevance and broader implications ==
== Important amino acids==
== Important amino acids==
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In the protein seen in the paper there is a mutation at residue 54, causing an <scene name='89/892740/Mutation_scence/1'>aspartic acid to change to an alanine</scene>. The catalytic amino acids are <scene name='89/892740/Catalytic_amino_acids/1'>Thr 312, Lys 270, Ser 268, Glu 269, Ser 157, Asp 156, Thr 158, Ala 291, Lys 294, and Thr 313</scene>.
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== Structural highlights ==
== Structural highlights ==
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In the protein seen in the paper there is a mutation at residue 54, causing an <scene name='89/892740/Mutation_scence/1'>aspartic acid to change to an alanine</scene>. The catalytic amino acids are <scene name='89/892740/Catalytic_amino_acids/1'>Thr 312, Lys 270, Ser 268, Glu 269, Ser 157, Asp 156, Thr 158, Ala 291, Lys 294, and Thr 313</scene>.
This protein is a mutation of 1INP, it has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate and ligand. The structure is <scene name='89/892740/Secondary_structures/1'>77% helix and 23% beta sheet</scene>, the betta sheets allow for twisting of the molecule so that the ligand better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions. <ref> PMID 33172890 </ref>
This protein is a mutation of 1INP, it has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate and ligand. The structure is <scene name='89/892740/Secondary_structures/1'>77% helix and 23% beta sheet</scene>, the betta sheets allow for twisting of the molecule so that the ligand better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions. <ref> PMID 33172890 </ref>

Revision as of 17:25, 3 December 2021

This Sandbox is Reserved from 10/01/2021 through 01/01//2022 for use in Biochemistry taught by Bonnie Hall at Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1690 through Sandbox Reserved 1699.
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7KIR

Inositol plyphosphate 1-phosphatase

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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
  3. ↑ Dollins DE, Xiong JP, Endo-Streeter S, Anderson DE, Bansal VS, Ponder JW, Ren Y, York JD. A Structural Basis for Lithium and Substrate Binding of an Inositide Phosphatase. J Biol Chem. 2020 Nov 10. pii: RA120.014057. doi: 10.1074/jbc.RA120.014057. PMID:33172890 doi:http://dx.doi.org/10.1074/jbc.RA120.014057
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