1f2v: Difference between revisions

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[[Image:1f2v.jpg|left|200px]]<br /><applet load="1f2v" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1f2v.jpg|left|200px]]<br /><applet load="1f2v" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1f2v, resolution 2.1Å" />

'''CRYSTAL STRUCTURE ANALYSIS OF PRECORRIN-8X METHYLMUTASE OF AEROBIC VITAMIN B12 SYNTHESIS'''<br />

==Overview==

BACKGROUND: The crystal structure of precorrin-8x methyl mutase (CobH), an, enzyme of the aerobic pathway to vitamin B12, provides evidence that the, mechanism for methyl migration can plausibly be regarded as an allowed, [1,5]-sigmatropic shift of a methyl group from C-11 to C-12 at the C ring, of precorrin-8x to afford hydrogenobyrinic acid. RESULTS: The dimeric, structure of CobH creates a set of shared active sites that readily, discriminate between different tautomers of precorrin-8x and select a, discrete tautomer for sigmatropic rearrangement. The active site contains, a strictly conserved histidine residue close to the site of methyl, migration in ring C of the substrate. CONCLUSION: Analysis of the, structure with bound product suggests that the [1,5]-sigmatropic shift, proceeds by protonation of the ring C nitrogen, leading to subsequent, methyl migration.

BACKGROUND: The crystal structure of precorrin-8x methyl mutase (CobH), an enzyme of the aerobic pathway to vitamin B12, provides evidence that the mechanism for methyl migration can plausibly be regarded as an allowed [1,5]-sigmatropic shift of a methyl group from C-11 to C-12 at the C ring of precorrin-8x to afford hydrogenobyrinic acid. RESULTS: The dimeric structure of CobH creates a set of shared active sites that readily discriminate between different tautomers of precorrin-8x and select a discrete tautomer for sigmatropic rearrangement. The active site contains a strictly conserved histidine residue close to the site of methyl migration in ring C of the substrate. CONCLUSION: Analysis of the structure with bound product suggests that the [1,5]-sigmatropic shift proceeds by protonation of the ring C nitrogen, leading to subsequent methyl migration.

==About this Structure==

1F2V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_denitrificans Pseudomonas denitrificans]. Active as [http://en.wikipedia.org/wiki/Precorrin-8X_methylmutase Precorrin-8X methylmutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.1.2 5.4.1.2] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1F2V OCA].

1F2V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_denitrificans Pseudomonas denitrificans]. Active as [http://en.wikipedia.org/wiki/Precorrin-8X_methylmutase Precorrin-8X methylmutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.1.2 5.4.1.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F2V OCA].

==Reference==

Line 15:

[[Category: Single protein]]

[[Category: Li, D.]]

[[Category: Roessner, C.A.]]

[[Category: Roessner, C A.]]

[[Category: Sacchettini, J.C.]]

[[Category: Sacchettini, J C.]]

[[Category: Scott, A.I.]]

[[Category: Scott, A I.]]

[[Category: Shipman, L.W.]]

[[Category: Shipman, L W.]]

[[Category: alpha-beta wind]]

[[Category: doubly wound sheet]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 14~~:33:~~38 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:34:13 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1f2v.jpg|left|200px]]<br /><applet load="1f2v" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1f2v.jpg|left|200px]]<br /><applet load="1f2v" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1f2v, resolution 2.1&Aring;" />
 '''CRYSTAL STRUCTURE ANALYSIS OF PRECORRIN-8X METHYLMUTASE OF AEROBIC VITAMIN B12 SYNTHESIS'''<br />
 ==Overview==
-BACKGROUND: The crystal structure of precorrin-8x methyl mutase (CobH), an, enzyme of the aerobic pathway to vitamin B12, provides evidence that the, mechanism for methyl migration can plausibly be regarded as an allowed, [1,5]-sigmatropic shift of a methyl group from C-11 to C-12 at the C ring, of precorrin-8x to afford hydrogenobyrinic acid. RESULTS: The dimeric, structure of CobH creates a set of shared active sites that readily, discriminate between different tautomers of precorrin-8x and select a, discrete tautomer for sigmatropic rearrangement. The active site contains, a strictly conserved histidine residue close to the site of methyl, migration in ring C of the substrate. CONCLUSION: Analysis of the, structure with bound product suggests that the [1,5]-sigmatropic shift, proceeds by protonation of the ring C nitrogen, leading to subsequent, methyl migration.
+BACKGROUND: The crystal structure of precorrin-8x methyl mutase (CobH), an enzyme of the aerobic pathway to vitamin B12, provides evidence that the mechanism for methyl migration can plausibly be regarded as an allowed [1,5]-sigmatropic shift of a methyl group from C-11 to C-12 at the C ring of precorrin-8x to afford hydrogenobyrinic acid. RESULTS: The dimeric structure of CobH creates a set of shared active sites that readily discriminate between different tautomers of precorrin-8x and select a discrete tautomer for sigmatropic rearrangement. The active site contains a strictly conserved histidine residue close to the site of methyl migration in ring C of the substrate. CONCLUSION: Analysis of the structure with bound product suggests that the [1,5]-sigmatropic shift proceeds by protonation of the ring C nitrogen, leading to subsequent methyl migration.
 ==About this Structure==
-F2V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_denitrificans Pseudomonas denitrificans]. Active as [http://en.wikipedia.org/wiki/Precorrin-8X_methylmutase Precorrin-8X methylmutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.1.2 5.4.1.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F2V OCA].
+F2V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_denitrificans Pseudomonas denitrificans]. Active as [http://en.wikipedia.org/wiki/Precorrin-8X_methylmutase Precorrin-8X methylmutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.1.2 5.4.1.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F2V OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Single protein]]
 [[Category: Li, D.]]
-[[Category: Roessner, C.A.]]
+[[Category: Roessner, C A.]]
-[[Category: Sacchettini, J.C.]]
+[[Category: Sacchettini, J C.]]
-[[Category: Scott, A.I.]]
+[[Category: Scott, A I.]]
-[[Category: Shipman, L.W.]]
+[[Category: Shipman, L W.]]
 [[Category: alpha-beta wind]]
 [[Category: doubly wound sheet]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:33:38 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:34:13 2008''