Sandbox Reserved 640: Difference between revisions

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The 16 kDa polypeptide leghemoglobin consists of two main subunits, the main globin structure and the iron-encompassing heme (protoporphyrin XI) group. These two subunits form a molecule structurally similar to Myoglobin <ref name=a />. The globin fold portion of the molecule is the standard globin secondary structure, a series of <scene name='Sandbox_Reserved_640/Alpha_helices/1'>8 alpha helices</scene> ~~(Ref 5)~~. Depending on the species and specific type of Leghemoglobin, the primary amino acid sequence can differ some, but overall it is well conserved.

The 16 kDa polypeptide leghemoglobin consists of two main subunits, the main globin structure and the iron-encompassing heme (protoporphyrin XI) group. These two subunits form a molecule structurally similar to Myoglobin <ref name=a />. The globin fold portion of the molecule is the standard globin secondary structure, a series of <scene name='Sandbox_Reserved_640/Alpha_helices/1'>8 alpha helices</scene> <ref name=five />. Depending on the species and specific type of Leghemoglobin, the primary amino acid sequence can differ some, but overall it is well conserved.

The <scene name='Sandbox_Reserved_640/Heme/1'>heme</scene> prosthetic group consists of four 5-membered pyrrole rings, forming a cyclic ring around a central iron (Fe) atom. This atom is contained within four equatorial nitrogens, in addition to another nitrogen from a close histidine residue and an opposite dioxygen (Ref 9). The ligand contact residues along the heme group are Phe30, <scene name='Sandbox_Reserved_640/His63/1'>His63</scene>, and Val67. Depending on the specific type of Leghemoglobin, some of these specific residues are disordered and others interconvert between two conformations (Ref 7).

Sandbox Reserved 640: Difference between revisions

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 <Structure load='2GDM' size='350' frame='true' align='right' caption='Structure of Leghemoglobin' scene='Insert optional scene name here' />
-The 16 kDa polypeptide leghemoglobin consists of two main subunits, the main globin structure and the iron-encompassing heme (protoporphyrin XI) group.  These two subunits form a molecule structurally similar to Myoglobin <ref name=a />.  The globin fold portion of the molecule is the standard globin secondary structure, a series of <scene name='Sandbox_Reserved_640/Alpha_helices/1'>8 alpha helices</scene> (Ref 5).  Depending on the species and specific type of Leghemoglobin, the primary amino acid sequence can differ some, but overall it is well conserved.
+The 16 kDa polypeptide leghemoglobin consists of two main subunits, the main globin structure and the iron-encompassing heme (protoporphyrin XI) group.  These two subunits form a molecule structurally similar to Myoglobin <ref name=a />.  The globin fold portion of the molecule is the standard globin secondary structure, a series of <scene name='Sandbox_Reserved_640/Alpha_helices/1'>8 alpha helices</scene> <ref name=five />.  Depending on the species and specific type of Leghemoglobin, the primary amino acid sequence can differ some, but overall it is well conserved.
 The <scene name='Sandbox_Reserved_640/Heme/1'>heme</scene> prosthetic group consists of four 5-membered pyrrole rings, forming a cyclic ring around a central iron (Fe) atom.  This atom is contained within four equatorial nitrogens, in addition to another nitrogen from a close histidine residue and an opposite dioxygen (Ref 9).  The ligand contact residues along the heme group are Phe30, <scene name='Sandbox_Reserved_640/His63/1'>His63</scene>, and Val67.  Depending on the specific type of Leghemoglobin, some of these specific residues are disordered and others interconvert between two conformations (Ref 7).