1v7l: Difference between revisions

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[[Image:1v7l.jpg|left|200px]]
{{Seed}}
[[Image:1v7l.png|left|200px]]


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{{STRUCTURE_1v7l|  PDB=1v7l  |  SCENE=  }}  
{{STRUCTURE_1v7l|  PDB=1v7l  |  SCENE=  }}  


'''Structure of 3-isopropylmalate isomerase small subunit from Pyrococcus horikoshii'''
===Structure of 3-isopropylmalate isomerase small subunit from Pyrococcus horikoshii===




==Overview==
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Recent studies have implied that the isopropylmalate isomerase small subunit of the hyperthermophilic archaea Pyrococcus horikoshii (PhIPMI-s) functions as isopropylmalate isomerase in the leucine biosynthesis pathway, and as homoaconitase (HACN) in the lysine biosynthesis pathway via alpha-aminoadipic acid. PhIPMI is thus considered a key to understanding the fundamental metabolism of the earliest organisms. We describe for the first time the crystal structure of PhIPMI-s, which displays dual substrate specificity. The crystal structure unexpectedly shows that four molecules create an interlocked assembly with intermolecular disulfide linkages having a skewed 222 point-group symmetry. Although the overall fold of the PhIPMI-s monomer is related closely to domain 4 of the aconitase (ACN), one alpha-helix in the ACN structure is replaced by a short loop with relatively high temperature factor values. Because this region is essential for discriminating the structurally similar substrate based on interactions with its diversified gamma-moiety, the loop structure in the PhIPMI-s must be dependent on the presence of a substrate. The flexibility of the loop region might be a structural basis for recognizing both hydrophobic and hydrophilic gamma-moieties of two distinct substrates, isopropylmalate and homocitrate.
The line below this paragraph, {{ABSTRACT_PUBMED_15522288}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_15522288}}


==About this Structure==
==About this Structure==
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[[Category: Yao, M.]]
[[Category: Yao, M.]]
[[Category: Beta barrel]]
[[Category: Beta barrel]]
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