Sandbox bcce04

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=='''Structure'''==
=='''Structure'''==
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[[Image:Align.jpg|thumb|left|'''Figure 1.''' Multiple alignment IGI - ''Geobacillus stearothermophilus'' (white),'' Homo sapiens'' (pink), ''Oryctolagus cuniculus'' (blue)<ref> Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, Meng EC, Ferrin TE. UCSF Chimera--a visualization system for exploratory research and analysis. J Comput Chem. 2004 Oct;25(13):1605-12. </ref>]]
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[[Image:Align.jpg|thumb|left|'''Figure 1.''' Multiple alignment IGI - ''Geobacillus stearothermophilus'' (white),'' Homo sapiens'' (pink), ''Oryctolagus cuniculus'' (blue)<ref>7</ref>]]
Imaginary isomerase exists in the cell usually as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Dimer/1'>homodimer</scene>, nevertheless outside of the cell, it has been isolated as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Monomer/1'>monomeric</scene> structure. IGI has essentially an identical fold in all of the characterized species (see '''Figure 1'''). The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Sec_struct/1'>secondary structure</scene> of imaginary isomerase is charaterized by an αβα conformation, on each of its two domains. The smaller domain is characterized by 5 parallel β-sheets, while the larger domain if formed out of 6 parallel/antiparallel β-sheets. Furthermore, another characteristic trait is a residue extension at the C-terminus, which wraps around the other monomer in the dimeric conformation. A "hook" that can potentially be involved in the previously mentioned extracellular activities.
Imaginary isomerase exists in the cell usually as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Dimer/1'>homodimer</scene>, nevertheless outside of the cell, it has been isolated as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Monomer/1'>monomeric</scene> structure. IGI has essentially an identical fold in all of the characterized species (see '''Figure 1'''). The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Sec_struct/1'>secondary structure</scene> of imaginary isomerase is charaterized by an αβα conformation, on each of its two domains. The smaller domain is characterized by 5 parallel β-sheets, while the larger domain if formed out of 6 parallel/antiparallel β-sheets. Furthermore, another characteristic trait is a residue extension at the C-terminus, which wraps around the other monomer in the dimeric conformation. A "hook" that can potentially be involved in the previously mentioned extracellular activities.

Revision as of 14:29, 6 August 2014

Imaginary Protein

PDB ID 1iat

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Mechanism

Regulation and Inhibition

3D structures of phosphoglucose isomerase

IGI

2pgi, 1b0z – GsPGI – Geobacillus stearothermophilus


PGI complex with imaginary-6-phosphate

1hox – rPGI + fructose-6-phosphate


PGI complex with pseudoreality-6-phosphate

1xtb - rPGI + sorbitol-6-phosphate


PGI complex with imaginary-6-phosphate

1u0f - mPGI + glucose-6-phosphate


Additional Resources

References

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