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| | ==C.lacteus nerve Hb in complex with CO== | | ==C.lacteus nerve Hb in complex with CO== |
| - | <StructureSection load='4avd' size='340' side='right' caption='[[4avd]], [[Resolution|resolution]] 1.50Å' scene=''> | + | <StructureSection load='4avd' size='340' side='right'caption='[[4avd]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4avd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cerla Cerla]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AVD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AVD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4avd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cerebratulus_lacteus Cerebratulus lacteus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AVD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AVD FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kr7|1kr7]], [[1v07|1v07]], [[2vyy|2vyy]], [[2vyz|2vyz]], [[2xkg|2xkg]], [[2xkh|2xkh]], [[2xki|2xki]], [[4ave|4ave]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4avd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4avd OCA], [http://pdbe.org/4avd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4avd RCSB], [http://www.ebi.ac.uk/pdbsum/4avd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4avd ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4avd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4avd OCA], [https://pdbe.org/4avd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4avd RCSB], [https://www.ebi.ac.uk/pdbsum/4avd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4avd ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GLBN_CERLA GLBN_CERLA]] Acts as an oxygen store capable of sustaining neuronal activity in an anoxic environment for 5 to 30 min. | + | [https://www.uniprot.org/uniprot/GLBN_CERLA GLBN_CERLA] Acts as an oxygen store capable of sustaining neuronal activity in an anoxic environment for 5 to 30 min. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cerla]] | + | [[Category: Cerebratulus lacteus]] |
| - | [[Category: Bolognesi, M]] | + | [[Category: Large Structures]] |
| - | [[Category: Dewilde, S]] | + | [[Category: Bolognesi M]] |
| - | [[Category: Germani, F]] | + | [[Category: Dewilde S]] |
| - | [[Category: Moens, L]] | + | [[Category: Germani F]] |
| - | [[Category: Nardini, M]] | + | [[Category: Moens L]] |
| - | [[Category: Pesce, A]] | + | [[Category: Nardini M]] |
| - | [[Category: Venturini, A]] | + | [[Category: Pesce A]] |
| - | [[Category: Carbon monoxide]]
| + | [[Category: Venturini A]] |
| - | [[Category: Heme reactivity]]
| + | |
| - | [[Category: Nerve globin]]
| + | |
| - | [[Category: Oxygen transport]]
| + | |
| - | [[Category: Protein matrix tunnel]]
| + | |
| Structural highlights
4avd is a 1 chain structure with sequence from Cerebratulus lacteus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.5Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
GLBN_CERLA Acts as an oxygen store capable of sustaining neuronal activity in an anoxic environment for 5 to 30 min.
Publication Abstract from PubMed
The nerve tissue mini-hemoglobin from Cerebratulus lacteus (CerHb) displays an essential globin fold hosting a protein matrix tunnel held to allow traffic of small ligands to and from the heme. CerHb heme pocket hosts the distal TyrB10/GlnE7 pair, normally linked to low rates of O(2) dissociation and ultra-high O(2) affinity. However, CerHb affinity for O(2) is similar to that of mammalian myoglobins, due to a dynamic equilibrium between high and low affinity states driven by the ability of ThrE11 to orient the TyrB10 OH group relative to the heme ligand. We present here the high resolution crystal structures of CerHb in the unligated and carbomonoxy states. Although CO binds to the heme with an orientation different from the O(2) ligand, the overall binding schemes for CO and O(2) are essentially the same, both ligands being stabilized through a network of hydrogen bonds based on TyrB10, GlnE7, and ThrE11. No dramatic protein structural changes are needed to support binding of the ligands, which can freely reach the heme distal site through the apolar tunnel. A lack of main conformational changes between the heme-unligated and -ligated states grants stability to the folded mini-Hb and is a prerequisite for fast ligand diffusion to/from the heme.
High Resolution Crystal Structures of the Cerebratulus lacteus Mini-Hb in the Unligated and Carbomonoxy States.,Germani F, Pesce A, Venturini A, Moens L, Bolognesi M, Dewilde S, Nardini M Int J Mol Sci. 2012;13(7):8025-37. doi: 10.3390/ijms13078025. Epub 2012 Jun 28. PMID:22942687[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Germani F, Pesce A, Venturini A, Moens L, Bolognesi M, Dewilde S, Nardini M. High Resolution Crystal Structures of the Cerebratulus lacteus Mini-Hb in the Unligated and Carbomonoxy States. Int J Mol Sci. 2012;13(7):8025-37. doi: 10.3390/ijms13078025. Epub 2012 Jun 28. PMID:22942687 doi:http://dx.doi.org/10.3390/ijms13078025
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