Sandbox Reserved 349: Difference between revisions

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==Structure==

PBGD is a monomeric three-domain polypeptide with each domain consisting of approximately 110 amino acids. The human variant has an additional 29 residue loop in domain three that extends hydrogen bonding across domains one and three while ''E.coli'' PBGD is lacking this extended loop <ref name="Raj">PMID: 19207107</ref>. In the active site, a unique molecule known as <scene name='Template:Sandbox_Reserved_349/~~Dpm_site~~/3'>Dipyrromethane</scene> interacts with porphobilinogen and anchors it in place<ref name="Raj">PMID: 19207107</ref>. Ordered <scene name='Sandbox_Reserved_349/So4_hbond/1'>sulfate ions</scene> are also hydrogen bonded with Arg26 and Ser28 residues near the active site that are highly conserved amongst human and ''E.coli'' variants of PBGD<ref name="Raj">PMID: 19207107</ref>.

PBGD is a monomeric three-domain polypeptide with each domain consisting of approximately 110 amino acids. The human variant has an additional 29 residue loop in domain three that extends hydrogen bonding across domains one and three while ''E.coli'' PBGD is lacking this extended loop <ref name="Raj">PMID: 19207107</ref>. In the active site, a unique molecule known as <scene name='Template:Sandbox_Reserved_349/Dpm/3'>Dipyrromethane</scene> interacts with porphobilinogen and anchors it in place<ref name="Raj">PMID: 19207107</ref>. Ordered <scene name='Sandbox_Reserved_349/So4_hbond/1'>sulfate ions</scene> are also hydrogen bonded with Arg26 and Ser28 residues near the active site that are highly conserved amongst human and ''E.coli'' variants of PBGD<ref name="Raj">PMID: 19207107</ref>.

Although PBGD appears to have hydrogen bonding capabilities between two identical PBGD units, at physiological pH, these interactions account for a dimer interface of approximately 5% while average dimer interface between subunits is 16%<ref name="Raj">PMID: 19207107</ref>. Therefore, it is generally assumed that this protein is active naturally as a monomeric enzyme, while the crystalline form is a homo-dimeric structure of two identical PBGD subunits<ref name="Raj">PMID: 19207107</ref>.

==Function==

Sandbox Reserved 349: Difference between revisions

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 ==Structure==
 <Structure load='3eq1' size='250' frame='true' align='left' scene='Sandbox_Reserved_349/Dpm/2' />
-PBGD is a monomeric three-domain polypeptide with each domain consisting of approximately 110 amino acids. The human variant has an additional 29 residue loop in domain three that extends hydrogen bonding across domains one and three while ''E.coli'' PBGD is lacking this extended loop <ref name="Raj">PMID: 19207107</ref>. In the active site, a unique molecule known as <scene name='Template:Sandbox_Reserved_349/Dpm_site/3'>Dipyrromethane</scene> interacts with porphobilinogen and anchors it in place<ref name="Raj">PMID: 19207107</ref>. Ordered <scene name='Sandbox_Reserved_349/So4_hbond/1'>sulfate ions</scene> are also hydrogen bonded with Arg26 and Ser28 residues near the active site that are highly conserved amongst human and ''E.coli'' variants of PBGD<ref name="Raj">PMID: 19207107</ref>.
+PBGD is a monomeric three-domain polypeptide with each domain consisting of approximately 110 amino acids. The human variant has an additional 29 residue loop in domain three that extends hydrogen bonding across domains one and three while ''E.coli'' PBGD is lacking this extended loop <ref name="Raj">PMID: 19207107</ref>. In the active site, a unique molecule known as <scene name='Template:Sandbox_Reserved_349/Dpm/3'>Dipyrromethane</scene> interacts with porphobilinogen and anchors it in place<ref name="Raj">PMID: 19207107</ref>. Ordered <scene name='Sandbox_Reserved_349/So4_hbond/1'>sulfate ions</scene> are also hydrogen bonded with Arg26 and Ser28 residues near the active site that are highly conserved amongst human and ''E.coli'' variants of PBGD<ref name="Raj">PMID: 19207107</ref>.
 Although PBGD appears to have hydrogen bonding capabilities between two identical PBGD units, at physiological pH, these interactions account for a dimer interface of approximately 5% while average dimer interface between subunits is 16%<ref name="Raj">PMID: 19207107</ref>. Therefore, it is generally assumed that this protein is active naturally as a monomeric enzyme, while the crystalline form is a homo-dimeric structure of two identical PBGD subunits<ref name="Raj">PMID: 19207107</ref>.
 ==Function==