InhA

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<StructureSection load='2h9i' size='450' side='right' scene='' caption=''>
='''InhA'''=
='''InhA'''=
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by Kelly Hrywkiw
by Kelly Hrywkiw
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{{STRUCTURE_2h9i | PDB=2h9i | SCENE= }}
 
__TOC__
__TOC__
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=Introduction=
=Introduction=
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=Structure of InhA=
=Structure of InhA=
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[[Image:Stero veiw.png|thumb|right|upright=2.5|alt=Secondary Structure Succession of InhA. Secondary structure residues are ordered from blue to red.|Fig.1: Stero view of the homotetramer structure of InhA with secondary structure succession outlined]]
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<scene name='Sandbox_Reserved_321/Structural_progresion/1'>Momomeric subunit of InhA with bound EAD</scene>
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[[Image:Stero veiw.png|thumb|left|upright=2.5|alt=Secondary Structure Succession of InhA. Secondary structure residues are ordered from blue to red.|Fig.1: Stero view of the homotetramer structure of InhA with secondary structure succession outlined]]
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<Structure load='2h9i' size='275' frame='true' align='left' caption='Momomeric subunit of InhA with bound EAD' scene='Sandbox_Reserved_321/Structural_progresion/1' />
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The InhA enzyme of ''M. tuberculosis'' is a homotetramer (Fig. 1) composed of a repeating subunit of a single domain with a [http://en.wikipedia.org/wiki/Rossmann_fold Rossmann Fold] in the core that provides a NADH binding site<ref name ="crystallographic studies"/>. The single domain can be broken down into two substructures that are connected by short peptide loop<ref name ="making drugs for inhA"/><ref name ="crystallographic studies">PMID:17588773</ref>. The overall structure exhibits α/β folding with a series of [http://en.wikipedia.org/wiki/Alpha_helix α helices] flanking a central [http://en.wikipedia.org/wiki/Beta_sheet β sheet] of multiple parallel β strands<ref name ="crystallographic studies"/>.
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The InhA enzyme <scene name='Sandbox_Reserved_321/Structural_progresion/1'>(go to original scene)</scene> of ''M. tuberculosis'' is a homotetramer (Fig. 1) composed of a repeating subunit of a single domain with a [http://en.wikipedia.org/wiki/Rossmann_fold Rossmann Fold] in the core that provides a NADH binding site<ref name ="crystallographic studies"/>. The single domain can be broken down into two substructures that are connected by short peptide loop<ref name ="making drugs for inhA"/><ref name ="crystallographic studies">PMID:17588773</ref>. The overall structure exhibits α/β folding with a series of [http://en.wikipedia.org/wiki/Alpha_helix α helices] flanking a central [http://en.wikipedia.org/wiki/Beta_sheet β sheet] of multiple parallel β strands<ref name ="crystallographic studies"/>.
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==Substructure 1 of InhA==
==Substructure 1 of InhA==
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=InhA's Function in the Mycolic Acid Pathway=
=InhA's Function in the Mycolic Acid Pathway=
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[[Image:Pathway2.png|thumb|right|upright=2|alt=Proposed mechanism.|Fig 2: Formulated mechanism of Mycolic acid synthesis as proposed by Wilson et al.<ref name ="Drug Induced Alterations">PMID:10536008</ref>.]]
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[[Image:Pathway2.png|thumb|left|upright=2|alt=Proposed mechanism.|Fig 2: Formulated mechanism of Mycolic acid synthesis as proposed by Wilson et al.<ref name ="Drug Induced Alterations">PMID:10536008</ref>.]]
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{{Clear}}
InhA plays a key role in the synthesis of fatty acids, particularly in ''M. tuberculosis'' which, has type one fatty acid synthesis (FASI) and type two fatty acid synthesis (FASII) which together function in the synthesis of mycolic acids<ref name ="Function of M Tb">PMID:18552191</ref>. FASI synthesizes C16-18 and C24-26 fatty acids. The fatty acids from FASI are then sent to FASII which promotes chain extension, forming long-chain meromycolic acids that are 56-64 carbons in length<ref name ="Fatty Acid Synthesis">PMID:18804030</ref>. The final step in FASII is completed by InhA which reduces 2-trans-enoyl-ACP's with chain lengths over twelve carbons in a NADP dependent manner where the hydride transfer precedes protonation(Fig. 2)<ref name ="Function of M Tb"/><ref name ="Roles of T158">PMID:10521269</ref>.
InhA plays a key role in the synthesis of fatty acids, particularly in ''M. tuberculosis'' which, has type one fatty acid synthesis (FASI) and type two fatty acid synthesis (FASII) which together function in the synthesis of mycolic acids<ref name ="Function of M Tb">PMID:18552191</ref>. FASI synthesizes C16-18 and C24-26 fatty acids. The fatty acids from FASI are then sent to FASII which promotes chain extension, forming long-chain meromycolic acids that are 56-64 carbons in length<ref name ="Fatty Acid Synthesis">PMID:18804030</ref>. The final step in FASII is completed by InhA which reduces 2-trans-enoyl-ACP's with chain lengths over twelve carbons in a NADP dependent manner where the hydride transfer precedes protonation(Fig. 2)<ref name ="Function of M Tb"/><ref name ="Roles of T158">PMID:10521269</ref>.

Revision as of 07:46, 21 August 2013

PDB ID 2h9i

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Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, Michal Harel, Kelly Hrywkiw

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